Protein Quantity on the Air–Solid Interface Determines Degradation Rates of Human Growth Hormone in Lyophilized Samples

Recombinant human growth hormone (rhGH) was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass formation kinetics, associated relaxation processes, and glass-specific surface areas (SSAs). The secondary...

Full description

Saved in:
Bibliographic Details
Published inJournal of pharmaceutical sciences Vol. 103; no. 5; pp. 1356 - 1366
Main Authors Xu, Yemin, Grobelny, Pawel, Von Allmen, Alexander, Knudson, Korben, Pikal, Michael, Carpenter, John F., Randolph, Theodore W.
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.05.2014
Elsevier Limited
Subjects
annealing
Chemistry, Pharmaceutical - methods
Circular Dichroism - methods
Drug Stability
Freeze Drying - methods
Glass - chemistry
growth hormone
Human Growth Hormone - chemistry
Humans
lyophilization
mobility
Powders - chemistry
protein formulation
protein structure
Protein Structure, Secondary
Recombinant Proteins - chemistry
specific surface area
stability
surface degradation
Transition Temperature
Water - chemistry
protein structure
protein formulation
lyophilization
mobility
surface degradation
specific surface area
growth hormone
annealing
stability
Online AccessGet full text

Cover

Abstract Recombinant human growth hormone (rhGH) was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass formation kinetics, associated relaxation processes, and glass-specific surface areas (SSAs). The secondary structure in the cake was monitored by infrared and in reconstituted samples by circular dichroism. The rhGH concentrations on the surface of lyophilized powders were determined from electron spectroscopy for chemical analysis. Glass transition temperature (Tg), SSAs, and water contents were determined immediately after lyophilization. Lyophilized samples were incubated at 323K for 16weeks, and the resulting extents of rhGH aggregation, oxidation, and deamidation were determined after rehydration. Water contents and Tg were independent of lyophilization process parameters. Compared with samples lyophilized after rapid freezing, rhGH in samples that had been annealed in frozen solids prior to drying, or annealed in glassy solids after secondary drying retained more native-like protein secondary structure, had a smaller fraction of the protein on the surface of the cake, and exhibited lower levels of degradation during incubation. A simple kinetic model suggested that the differences in the extent of rhGH degradation during storage in the dried state between different formulations and processing methods could largely be ascribed to the associated levels of rhGH at the solid–air interface after lyophilization. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association.
AbstractList rhGH was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass formation kinetics, associated relaxation processes and glass specific surface areas (SSA’s). The secondary structure in the cake was monitored by IR and in reconstituted samples by CD. The rhGH concentrations on the surface of lyophilized powders were determined from ESCA. T g , SSA’s and water contents were determined immediately after lyophilization. Lyophilized samples were incubated at 323 K for 16 weeks, and the resulting extents of rhGH aggregation, oxidation and deamidation were determined after rehydration. Water contents and T g were independent of lyophilization process parameters. Compared to samples lyophilized after rapid freezing, rhGH in samples that had been annealed in frozen solids prior to drying, or annealed in glassy solids after secondary drying retained more native-like protein secondary structure, had a smaller fraction of the protein on the surface of the cake and exhibited lower levels of degradation during incubation. A simple kinetic model suggested that the differences in the extent of rhGH degradation during storage in the dried state between different formulations and processing methods could largely be ascribed to the associated levels of rhGH at the solid-air interface after lyophilization.
Recombinant human growth hormone (rhGH) was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass formation kinetics, associated relaxation processes, and glass-specific surface areas (SSAs). The secondary structure in the cake was monitored by infrared and in reconstituted samples by circular dichroism. The rhGH concentrations on the surface of lyophilized powders were determined from electron spectroscopy for chemical analysis. Glass transition temperature (Tg), SSAs, and water contents were determined immediately after lyophilization. Lyophilized samples were incubated at 323 K for 16 weeks, and the resulting extents of rhGH aggregation, oxidation, and deamidation were determined after rehydration. Water contents and Tg were independent of lyophilization process parameters. Compared with samples lyophilized after rapid freezing, rhGH in samples that had been annealed in frozen solids prior to drying, or annealed in glassy solids after secondary drying retained more native-like protein secondary structure, had a smaller fraction of the protein on the surface of the cake, and exhibited lower levels of degradation during incubation. A simple kinetic model suggested that the differences in the extent of rhGH degradation during storage in the dried state between different formulations and processing methods could largely be ascribed to the associated levels of rhGH at the solid-air interface after lyophilization. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association J Pharm Sci 103:1356-1366, 2014
Recombinant human growth hormone (rhGH) was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass formation kinetics, associated relaxation processes, and glass-specific surface areas (SSAs). The secondary structure in the cake was monitored by infrared and in reconstituted samples by circular dichroism. The rhGH concentrations on the surface of lyophilized powders were determined from electron spectroscopy for chemical analysis. Glass transition temperature (Tg ), SSAs, and water contents were determined immediately after lyophilization. Lyophilized samples were incubated at 323 K for 16 weeks, and the resulting extents of rhGH aggregation, oxidation, and deamidation were determined after rehydration. Water contents and Tg were independent of lyophilization process parameters. Compared with samples lyophilized after rapid freezing, rhGH in samples that had been annealed in frozen solids prior to drying, or annealed in glassy solids after secondary drying retained more native-like protein secondary structure, had a smaller fraction of the protein on the surface of the cake, and exhibited lower levels of degradation during incubation. A simple kinetic model suggested that the differences in the extent of rhGH degradation during storage in the dried state between different formulations and processing methods could largely be ascribed to the associated levels of rhGH at the solid-air interface after lyophilization.
Recombinant human growth hormone (rhGH) was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass formation kinetics, associated relaxation processes, and glass-specific surface areas (SSAs). The secondary structure in the cake was monitored by infrared and in reconstituted samples by circular dichroism. The rhGH concentrations on the surface of lyophilized powders were determined from electron spectroscopy for chemical analysis. Glass transition temperature (Tg), SSAs, and water contents were determined immediately after lyophilization. Lyophilized samples were incubated at 323K for 16weeks, and the resulting extents of rhGH aggregation, oxidation, and deamidation were determined after rehydration. Water contents and Tg were independent of lyophilization process parameters. Compared with samples lyophilized after rapid freezing, rhGH in samples that had been annealed in frozen solids prior to drying, or annealed in glassy solids after secondary drying retained more native-like protein secondary structure, had a smaller fraction of the protein on the surface of the cake, and exhibited lower levels of degradation during incubation. A simple kinetic model suggested that the differences in the extent of rhGH degradation during storage in the dried state between different formulations and processing methods could largely be ascribed to the associated levels of rhGH at the solid–air interface after lyophilization. © 2014 Wiley Periodicals, Inc. and the American Pharmacists Association.
Author Von Allmen, Alexander
Xu, Yemin
Grobelny, Pawel
Carpenter, John F.
Randolph, Theodore W.
Knudson, Korben
Pikal, Michael
AuthorAffiliation 4 Center for Pharmaceutical Biotechnology, Department of Pharmaceutical Sciences, University of Colorado Denver, Anschutz Medical Campus, Aurora, Colorado 80045
3 Center for Pharmaceutical Biotechnology, Department of Chemical and Biological Engineering, University of Colorado, Campus Box 596, Boulder, Colorado 80309
2 Department of Pharmaceutical Sciences, University of Connecticut, Storrs, Connecticut 06269
1 Center for Pharmaceutical Biotechnology, Department of Biochemistry, University of Colorado, Campus Box 596, Boulder, Colorado 80309
AuthorAffiliation_xml – name: 3 Center for Pharmaceutical Biotechnology, Department of Chemical and Biological Engineering, University of Colorado, Campus Box 596, Boulder, Colorado 80309
– name: 1 Center for Pharmaceutical Biotechnology, Department of Biochemistry, University of Colorado, Campus Box 596, Boulder, Colorado 80309
– name: 2 Department of Pharmaceutical Sciences, University of Connecticut, Storrs, Connecticut 06269
– name: 4 Center for Pharmaceutical Biotechnology, Department of Pharmaceutical Sciences, University of Colorado Denver, Anschutz Medical Campus, Aurora, Colorado 80045
Author_xml – sequence: 1
  givenname: Yemin
  surname: Xu
  fullname: Xu, Yemin
  organization: Center for Pharmaceutical Biotechnology Department of Biochemistry University of Colorado Boulder Colorado 80309
– sequence: 2
  givenname: Pawel
  surname: Grobelny
  fullname: Grobelny, Pawel
  organization: Department of Pharmaceutical Sciences University of Connecticut Storrs Connecticut 06269
– sequence: 3
  givenname: Alexander
  surname: Von Allmen
  fullname: Von Allmen, Alexander
  organization: Center for Pharmaceutical Biotechnology Department of Chemical and Biological Engineering University of Colorado Boulder Colorado 80309
– sequence: 4
  givenname: Korben
  surname: Knudson
  fullname: Knudson, Korben
  organization: Center for Pharmaceutical Biotechnology Department of Chemical and Biological Engineering University of Colorado Boulder Colorado 80309
– sequence: 5
  givenname: Michael
  surname: Pikal
  fullname: Pikal, Michael
  organization: Department of Pharmaceutical Sciences University of Connecticut Storrs Connecticut 06269
– sequence: 6
  givenname: John F.
  surname: Carpenter
  fullname: Carpenter, John F.
  organization: Center for Pharmaceutical Biotechnology Department of Pharmaceutical Sciences University of Colorado Denver, Anschutz Medical Campus Aurora Colorado 80045
– sequence: 7
  givenname: Theodore W.
  surname: Randolph
  fullname: Randolph, Theodore W.
  email: theodore.randolph@colorado.edu
  organization: Center for Pharmaceutical Biotechnology Department of Chemical and Biological Engineering University of Colorado Boulder Colorado 80309
BackLink https://www.ncbi.nlm.nih.gov/pubmed/24623139$$D View this record in MEDLINE/PubMed
BookMark eNp1kc9u1DAQxi1URLeFAy-ALHGBQ1rbifPnglQV6BatRGHhbDnOuOtVYgfbaRVOvANvyJPgsm0FCE4eeX7z6Zv5DtCedRYQekrJESWEHW_HcMTyhpUP0IJyRrKS0GoPLVKPZTkvmn10EMKWEFISzh-hfVaULKd5s0DzhXcRjMUfJmmjiTN2FscN4BPjf3z7vna96fC5jeC1VIBfQ6oGYyGk8tLLTkaTBj7KmH6cxstpkBafeXcdN3jp_JCM4qS-mt24Mb35Ch1ey2HsITxGD7XsAzy5fQ_R57dvPp0us9X7s_PTk1WmiroqM82kBs6ZglrLRndUt6zsZFPzqi2qqm4V43nVViWpuKKyKiUQxSlpi66tG17mh-jVTnec2gE6BTZ62YvRm0H6WThpxJ8dazbi0l2JghQNqWkSeHEr4N2XCUIUgwkK-l5acFMQlNOccJbOmdDnf6FbN3mb1ruhaLJT50WiXu4o5V0IHvS9GUrETaAiBSp-BZrYZ7-7vyfvEkzA8Q64Nj3M_1cS7y7Wd5L5bgLS1a8MeBGUAaugMx5UFJ0z_zDyEx2lwKg
CODEN JPMSAE
CitedBy_id crossref_primary_10_2147_IJN_S245050
crossref_primary_10_1007_s11095_022_03358_z
crossref_primary_10_1016_j_xphs_2016_05_013
crossref_primary_10_1021_acs_molpharmaceut_6b00940
crossref_primary_10_1016_j_ijpharm_2021_120806
crossref_primary_10_1016_j_xphs_2018_02_003
crossref_primary_10_1016_j_xphs_2017_10_020
crossref_primary_10_1016_j_ijpharm_2021_120929
crossref_primary_10_1016_j_xphs_2024_05_014
crossref_primary_10_1016_j_xphs_2022_05_016
crossref_primary_10_1021_acs_molpharmaceut_9b00614
crossref_primary_10_1016_j_ejpb_2021_08_017
crossref_primary_10_1039_D4SM00028E
crossref_primary_10_1016_j_ijpharm_2023_122988
crossref_primary_10_1016_j_ejpb_2018_05_025
crossref_primary_10_1016_j_trac_2016_05_012
crossref_primary_10_1016_j_xphs_2016_04_035
crossref_primary_10_1016_j_addr_2015_05_006
crossref_primary_10_1016_j_xphs_2024_04_012
crossref_primary_10_1016_j_ejpb_2017_01_024
crossref_primary_10_1016_j_ijpharm_2018_09_057
crossref_primary_10_1063_5_0083726
crossref_primary_10_1016_j_ijpharm_2020_119448
crossref_primary_10_1016_j_addr_2016_01_005
crossref_primary_10_1021_acs_molpharmaceut_8b00935
crossref_primary_10_1016_j_xphs_2023_08_019
crossref_primary_10_1016_j_xphs_2019_10_010
crossref_primary_10_1002_jps_24171
crossref_primary_10_1016_j_bbagen_2022_130101
crossref_primary_10_1002_bip_22664
crossref_primary_10_1016_j_xphs_2016_04_020
crossref_primary_10_1002_btpr_3474
crossref_primary_10_1016_j_ijpharm_2022_122098
crossref_primary_10_1016_j_ijpharm_2023_123445
crossref_primary_10_1208_s12249_020_01794_x
crossref_primary_10_1016_j_xphs_2020_02_014
crossref_primary_10_1016_j_xphs_2020_02_019
crossref_primary_10_1016_j_ijpharm_2023_123084
Cites_doi 10.1002/jps.10334
10.1021/bi001547t
10.1002/(SICI)1097-0290(19990420)63:2<166::AID-BIT5>3.0.CO;2-H
10.1002/bit.22832
10.1126/science.267.5206.1924
10.1016/S1359-0278(98)00002-9
10.1002/jps.21768
10.1208/s12249-009-9338-7
10.1002/jps.22686
10.1021/bi001782b
10.1016/j.cis.2008.08.010
10.1023/A:1025771421906
10.1103/PhysRevLett.106.256103
10.1016/S0092-1157(82)80026-7
10.1016/S0378-5173(99)00226-4
10.1002/pro.5560060111
10.1023/A:1007568511399
10.1002/jps.23318
10.1021/js970135b
10.1002/polb.20919
10.1016/S0378-5173(00)00423-3
10.1023/A:1012180707283
10.1208/s12248-012-9345-6
10.1002/jps.1040
10.1021/js960080y
10.1002/jps.1039
10.1002/jps.10135
10.1039/c3sm51658j
10.1006/bbrc.1996.1364
10.1021/bp070462h
10.1103/PhysRevE.88.022601
10.1208/pt050458
10.1096/fasebj.10.1.8566549
10.1080/10837450701481157
10.1021/mp2004498
10.1016/S0939-6411(98)00005-8
10.1023/A:1016270103863
10.1016/j.ejpb.2013.03.036
10.1016/j.ejpb.2011.03.010
10.1023/A:1018828425184
10.1021/bi00207a018
10.1021/la0262349
10.1002/jps.21825
10.1002/jps.21085
10.1002/jps.22597
10.1038/nmat1484
10.1039/c2sm06979b
10.1103/PhysRevE.88.032601
10.1002/jps.21815
10.1016/S0927-7765(99)00042-9
10.1110/ps.42501
10.1002/pro.5560070611
10.1021/bm050353w
10.1023/A:1015929109894
10.1002/jps.21960
10.1016/j.ejpb.2013.04.003
10.1039/c3sm51251g
ContentType Journal Article
Copyright 2014 Wiley Periodicals, Inc. and the American Pharmacists Association
2014 Wiley Periodicals, Inc. and the American Pharmacists Association.
Copyright © 2014 Wiley Periodicals, Inc., A Wiley Company
Copyright_xml – notice: 2014 Wiley Periodicals, Inc. and the American Pharmacists Association
– notice: 2014 Wiley Periodicals, Inc. and the American Pharmacists Association.
– notice: Copyright © 2014 Wiley Periodicals, Inc., A Wiley Company
DBID CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QO
7QP
7QR
7TK
7U7
8FD
C1K
FR3
P64
RC3
7X8
5PM
DOI 10.1002/jps.23926
DatabaseName Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
CrossRef
Biotechnology Research Abstracts
Calcium & Calcified Tissue Abstracts
Chemoreception Abstracts
Neurosciences Abstracts
Toxicology Abstracts
Technology Research Database
Environmental Sciences and Pollution Management
Engineering Research Database
Biotechnology and BioEngineering Abstracts
Genetics Abstracts
MEDLINE - Academic
PubMed Central (Full Participant titles)
DatabaseTitle MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
CrossRef
Genetics Abstracts
Biotechnology Research Abstracts
Technology Research Database
Toxicology Abstracts
Chemoreception Abstracts
Engineering Research Database
Calcium & Calcified Tissue Abstracts
Neurosciences Abstracts
Biotechnology and BioEngineering Abstracts
Environmental Sciences and Pollution Management
MEDLINE - Academic
DatabaseTitleList
Genetics Abstracts
MEDLINE
Database_xml – sequence: 1
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
– sequence: 2
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Pharmacy, Therapeutics, & Pharmacology
EISSN 1520-6017
EndPage 1366
ExternalDocumentID 3263510941
10_1002_jps_23926
24623139
JPS23926
S0022354915305992
Genre article
Journal Article
Research Support, N.I.H., Extramural
GrantInformation_xml – fundername: NIBIB NIH HHS
  grantid: R01 EB006398-01A1
– fundername: NIBIB NIH HHS
  grantid: R01 EB006398
– fundername: NIBIB NIH HHS
  grantid: R01 EB006006
GroupedDBID ---
-~X
.3N
.GA
.GJ
.Y3
05W
0R~
10A
1CY
1L6
1OC
1ZS
31~
33P
36B
3O-
3WU
4.4
457
4ZD
50Y
50Z
51W
51X
52M
52N
52O
52P
52S
52T
52W
52X
53G
5GY
5RE
5VS
66C
702
7PT
8-0
8-1
8-3
8-4
8-5
8UM
930
A03
A8Z
AAEVG
AAHHS
AAIAV
AAKUH
AALRI
AAOIN
AAONW
AAXUO
AAYOK
AAZKR
ABCQN
ABEML
ABFRF
ABIJN
ABJNI
ABMAC
ABOCM
ABPVW
ABWRO
ACBWZ
ACCFJ
ACGFO
ACGFS
ACIWK
ACPRK
ACSCC
ACXME
ACXQS
ADBBV
ADIZJ
AEEZP
AEFWE
AEIMD
AENEX
AEQDE
AEUQT
AFBPY
AFFNX
AFRAH
AFTJW
AFZJQ
AGHFR
AI.
AITUG
AIWBW
AJAOE
AJBDE
ALAGY
ALMA_UNASSIGNED_HOLDINGS
AMBMR
AMRAJ
ATUGU
AZBYB
BAFTC
BDRZF
BFHJK
BNHUX
BROTX
BRXPI
BY8
CS3
D-E
D-F
DCZOG
DPXWK
DR2
DU5
E3Z
EBD
EBS
EJD
EMB
EMOBN
ESTFP
F00
F01
F04
F5P
FDB
FEDTE
G-S
G.N
GNP
GODZA
H.T
H.X
HBH
HF~
HHY
HHZ
HOLLA
HVGLF
HX~
HZ~
IX1
J0M
JPC
KQQ
L7B
LAW
LC2
LC3
LH4
LP6
LP7
LSO
LW6
M41
M6Q
MK0
MK4
N04
N05
N9A
NF~
NNB
O66
O9-
P2P
P2X
P4D
Q.N
Q11
QB0
QRW
R.K
RNS
ROL
RWI
RX1
RYL
SSZ
SUPJJ
SV3
UB1
UKR
UNMZH
V2E
V8K
VH1
W8V
W99
WBFHL
WH7
WIB
WJL
WQJ
WRC
WUP
WWP
WYUIH
XG1
XPP
XV2
Y6R
YCJ
ZE2
ZGI
ZXP
~IA
~WT
ADVLN
AKRWK
OIG
1OB
AFJKZ
CGR
CUY
CVF
ECM
EIF
NPM
AAYXX
CITATION
7QO
7QP
7QR
7TK
7U7
8FD
C1K
FR3
P64
RC3
7X8
5PM
ID FETCH-LOGICAL-c4876-f2afe552ce8fa9fd1fb26da9857b4778bc2537b76075c1a76ae0c510b4db89563
IEDL.DBID DR2
ISSN 0022-3549
IngestDate Tue Sep 17 21:17:46 EDT 2024
Thu Oct 24 23:35:41 EDT 2024
Thu Oct 10 22:17:30 EDT 2024
Thu Sep 26 16:21:31 EDT 2024
Sat Sep 28 08:01:13 EDT 2024
Sat Aug 24 00:54:03 EDT 2024
Fri Feb 23 02:31:01 EST 2024
IsDoiOpenAccess false
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 5
Keywords protein structure
protein formulation
lyophilization
mobility
surface degradation
specific surface area
growth hormone
annealing
stability
Language English
License 2014 Wiley Periodicals, Inc. and the American Pharmacists Association.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c4876-f2afe552ce8fa9fd1fb26da9857b4778bc2537b76075c1a76ae0c510b4db89563
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
OpenAccessLink https://europepmc.org/articles/pmc4049081?pdf=render
PMID 24623139
PQID 1511956834
PQPubID 1006386
PageCount 11
ParticipantIDs pubmedcentral_primary_oai_pubmedcentral_nih_gov_4049081
proquest_miscellaneous_1513052139
proquest_journals_1511956834
crossref_primary_10_1002_jps_23926
pubmed_primary_24623139
wiley_primary_10_1002_jps_23926_JPS23926
elsevier_sciencedirect_doi_10_1002_jps_23926
PublicationCentury 2000
PublicationDate May 2014
PublicationDateYYYYMMDD 2014-05-01
PublicationDate_xml – month: 05
  year: 2014
  text: May 2014
PublicationDecade 2010
PublicationPlace United States
PublicationPlace_xml – name: United States
– name: Washington
PublicationTitle Journal of pharmaceutical sciences
PublicationTitleAlternate J Pharm Sci
PublicationYear 2014
Publisher Elsevier Inc
Elsevier Limited
Publisher_xml – name: Elsevier Inc
– name: Elsevier Limited
References Bantchev, Schwartz (bb0245) 2003; 19
Searles, Carpenter, Randolph (bb0075) 2001; 90
Gabriele, Damman, Sclavons, Desprez, Coppee, Reiter, Hamieh, Al Akhrass, Vilmin, Raphael (bb0285) 2006; 44
Crisman, Randolph (bb0135) 2010; 107
Adler, Unger, Lee (bb0155) 2000; 17
Carpenter, Pikal, Chang, Randolph (bb0010) 1997; 14
Searles, Carpenter, Randolph (bb0060) 2001; 90
Patapoff, Overcashier (bb0110) 2002; 15
Rathore, Rajan (bb0065) 2008; 24
Chang, Pikal (bb0025) 2009; 98
Chieng, Mizuno, Pikal (bb0145) 2013; 85
Gomez-Orellana, Variano, Miura-Fraboni, Milstein, Paton (bb0215) 1998; 7
Speed, Morshead, Wang, King (bb0220) 1997; 6
Bee, Chiu, Sawicki, Stevenson, Chatterjee, Freund, Carpenter, Randolph (bb0270) 2009; 98
Randolph (bb0040) 1997; 86
Rambhatla, Ramot, Bhugra, Pikal (bb0095) 2004; 5
Zhu, Brian, Swallen, Straus, Ediger, Yu (bb0165) 2011; 106
Jiang, Li, Nguyen, Muzammil, Towers, Gabrielson, Narhi (bb0190) 2011; 100
Britt, Schwartz, Wurth, Mahler, Carpenter, Randolph (bb0265) 2012; 101
Liu, Orozco, Wang (bb0175) 2013; 88
Chi, Krishnan, Randolph, Carpenter (bb0240) 2003; 20
Carpenter, Prestrelski, Dong (bb0035) 1998; 45
Chieng, Cicerone, Zhong, Liu, Pikal (bb0150) 2013; 85
Webb, Cleland, Carpenter, Randolph (bb0100) 2003; 92
Heller, Carpenter, Randolph (bb0070) 1999; 63
May, Grim, Wheeler, West (bb0140) 1982; 10
Dickinson (bb0250) 1999; 15
Khurana, Gillespie, Talapatra, Minert, Ionescu-Zanetti, Millett, Fink (bb0195) 2001; 40
Abdul-Fattah, Lechuga-Ballesteros, Kalonia, Pikal (bb0050) 2008; 97
Millqvist-Fureby, Malmsten, Bergenstahl (bb0160) 1999; 188
Inoue, Nakamura, Matsui, Kanaya, Nishida, Hino (bb0290) 2013; 88
Fink, Calciano, Goto, Kurotsu, Palleros (bb0205) 1994; 33
Vessely, Carpenter, Schwartz (bb0260) 2005; 6
Manning, Patel, Borchardt (bb0015) 1989; 6
Patel, Bhugra, Pikal (bb0085) 2009; 10
Cochran, Nail (bb0090) 2009; 98
Kasper, Friess (bb0055) 2011; 78
Cicerone, Douglas (bb0030) 2012; 8
Sun, Zhu, Wu, Cai, Gunn, Yu (bb0295) 2012; 14
Angell (bb0180) 1995; 267
Xu, Carpenter, Cicerone, Randolph (bb0045) 2013; 9
Maa, Nguyen, Sweeney, Shire, Hsu (bb0125) 1999; 16
Reiter, Hamieh, Damman, Sclavons, Gabriele, Vilmin, Raphael (bb0280) 2005; 4
Carrotta, Bauer, Waninge, Rischel (bb0210) 2001; 10
Bhatnagar, Bogner, Pikal (bb0115) 2007; 12
Wang (bb0020) 2000; 203
Zuo, Liu, Wang, Zhu, Wang, Wang (bb0170) 2013; 9
Wang, Cicerone, Aso, Pikal (bb0130) 2010; 99
Kaminski, Adrjanowicz, Zakowiecki, Kaminska, Wlodarczyk, Paluch, Pilch, Tarnacka (bb0185) 2012; 9
Fink (bb0200) 1998; 3
Webb, Golledge, Cleland, Carpenter, Randolph (bb0080) 2002; 91
Kim, Yu (bb0230) 1996; 226
King, Haase-Pettingell, Robinson, Speed, Mitraki (bb0225) 1996; 10
Grillo, Edwards, Kashi, Shipley, Hu, Besman, Middaugh (bb0235) 2001; 40
Bee, Randolph, Carpenter, Bishop, Dimitrova (bb0275) 2011; 100
Hsu, Nguyen, Yeung, Brooks, Koe, Bewley, Pearlman (bb0105) 1995; 12
Chang, Kendrick, Carpenter (bb0120) 1996; 85
Krägel, Derkatch, Miller (bb0255) 2008; 144
2010; 99
2002; 15
2001; 90
2010; 107
1997; 86
1982; 10
2004; 5
2003; 19
2012; 14
1997; 6
2008; 144
1998; 45
2001; 40
2013; 9
1996; 226
2009; 98
2009; 10
2003; 92
2000; 17
2000; 203
1997; 14
1999; 16
1999; 15
1994; 33
2008; 24
2002; 91
2001; 10
2012; 101
2013; 88
1989; 6
1995; 12
2013; 85
2011; 78
1999; 63
1999; 188
2008; 97
2007; 12
1996; 10
2011; 106
2006; 44
2005; 4
1996; 85
2005; 6
1998; 3
1995; 267
1998; 7
2003; 20
2011; 100
2012; 8
2012; 9
7724490 - Pharm Res. 1995 Jan;12(1):69-77
23608636 - Eur J Pharm Biopharm. 2013 Oct;85(2):189-96
11458335 - J Pharm Sci. 2001 Jul;90(7):860-71
9655339 - Protein Sci. 1998 Jun;7(6):1352-8
18823871 - Adv Colloid Interface Sci. 2008 Dec 2;144(1-2):38-53
21770657 - Phys Rev Lett. 2011 Jun 24;106(25):256103
21523787 - J Pharm Sci. 2011 Oct;100(10):4158-70
17770101 - Science. 1995 Mar 31;267(5206):1924-35
19798764 - J Pharm Sci. 2010 Feb;99(2):683-700
11148054 - Biochemistry. 2001 Jan 16;40(2):586-95
18484778 - Biotechnol Prog. 2008 May-Jun;24(3):504-14
12661058 - J Pharm Sci. 2003 Apr;92(4):715-29
20589675 - Biotechnol Bioeng. 2010 Nov 1;107(4):663-72
7130203 - J Biol Stand. 1982 Jul;10(3):249-59
9383725 - J Pharm Sci. 1997 Nov;86(11):1198-203
19492408 - J Pharm Sci. 2009 Sep;98(9):3218-38
19569054 - J Pharm Sci. 2009 Sep;98(9):2886-908
10990207 - Pharm Res. 2000 Jul;17(7):863-70
17722086 - J Pharm Sci. 2008 Jan;97(1):163-84
8806643 - Biochem Biophys Res Commun. 1996 Sep 13;226(2):378-84
22987313 - J Pharm Sci. 2012 Dec;101(12):4419-32
9007981 - Protein Sci. 1997 Jan;6(1):99-108
7918473 - Biochemistry. 1994 Oct 18;33(41):12504-11
16283763 - Biomacromolecules. 2005 Nov-Dec;6(6):3334-44
10099593 - Biotechnol Bioeng. 1999 Apr 20;63(2):166-74
2687836 - Pharm Res. 1989 Nov;6(11):903-18
10518679 - Int J Pharm. 1999 Oct 25;188(2):243-53
11420433 - Protein Sci. 2001 Jul;10(7):1312-8
19937284 - AAPS PharmSciTech. 2009;10(4):1406-11
15760055 - AAPS PharmSciTech. 2004;5(4):e58
10100310 - Pharm Res. 1999 Feb;16(2):249-54
24125286 - Phys Rev E Stat Nonlin Soft Matter Phys. 2013 Sep;88(3):032601
22434258 - AAPS J. 2012 Sep;14(3):380-8
19492339 - J Pharm Sci. 2009 Sep;98(9):3495-8
23623797 - Eur J Pharm Biopharm. 2013 Oct;85(2):197-206
21426937 - Eur J Pharm Biopharm. 2011 Jun;78(2):248-63
14567625 - Pharm Res. 2003 Sep;20(9):1325-36
9502314 - Fold Des. 1998;3(1):R9-23
12115847 - J Pharm Sci. 2002 Jun;91(6):1474-87
22553901 - Mol Pharm. 2012 Jun 4;9(6):1559-69
10967427 - Int J Pharm. 2000 Aug 10;203(1-2):1-60
17963151 - Pharm Dev Technol. 2007;12(5):505-23
24032856 - Phys Rev E Stat Nonlin Soft Matter Phys. 2013 Aug;88(2):022601
21713773 - J Pharm Sci. 2011 Nov;100(11):4631-41
11458336 - J Pharm Sci. 2001 Jul;90(7):872-87
9279875 - Pharm Res. 1997 Aug;14(8):969-75
8566549 - FASEB J. 1996 Jan;10(1):57-66
9653627 - Eur J Pharm Biopharm. 1998 May;45(3):231-8
8961147 - J Pharm Sci. 1996 Dec;85(12):1325-30
16184173 - Nat Mater. 2005 Oct;4(10):754-8
11297418 - Biochemistry. 2001 Mar 27;40(12):3525-35
Patapoff (10.1002/jps.23926_bb0110) 2002; 15
Dickinson (10.1002/jps.23926_bb0250) 1999; 15
King (10.1002/jps.23926_bb0225) 1996; 10
Chieng (10.1002/jps.23926_bb0145) 2013; 85
Rambhatla (10.1002/jps.23926_bb0095) 2004; 5
Randolph (10.1002/jps.23926_bb0040) 1997; 86
Wang (10.1002/jps.23926_bb0020) 2000; 203
Grillo (10.1002/jps.23926_bb0235) 2001; 40
Krägel (10.1002/jps.23926_bb0255) 2008; 144
Gomez-Orellana (10.1002/jps.23926_bb0215) 1998; 7
Carpenter (10.1002/jps.23926_bb0035) 1998; 45
Cicerone (10.1002/jps.23926_bb0030) 2012; 8
Patel (10.1002/jps.23926_bb0085) 2009; 10
Fink (10.1002/jps.23926_bb0205) 1994; 33
May (10.1002/jps.23926_bb0140) 1982; 10
Kim (10.1002/jps.23926_bb0230) 1996; 226
Reiter (10.1002/jps.23926_bb0280) 2005; 4
Carrotta (10.1002/jps.23926_bb0210) 2001; 10
Searles (10.1002/jps.23926_bb0075) 2001; 90
Maa (10.1002/jps.23926_bb0125) 1999; 16
Liu (10.1002/jps.23926_bb0175) 2013; 88
Fink (10.1002/jps.23926_bb0200) 1998; 3
Jiang (10.1002/jps.23926_bb0190) 2011; 100
Millqvist-Fureby (10.1002/jps.23926_bb0160) 1999; 188
Hsu (10.1002/jps.23926_bb0105) 1995; 12
Adler (10.1002/jps.23926_bb0155) 2000; 17
Chang (10.1002/jps.23926_bb0120) 1996; 85
Heller (10.1002/jps.23926_bb0070) 1999; 63
Bee (10.1002/jps.23926_bb0270) 2009; 98
Crisman (10.1002/jps.23926_bb0135) 2010; 107
Xu (10.1002/jps.23926_bb0045) 2013; 9
Abdul-Fattah (10.1002/jps.23926_bb0050) 2008; 97
Webb (10.1002/jps.23926_bb0080) 2002; 91
Gabriele (10.1002/jps.23926_bb0285) 2006; 44
Carpenter (10.1002/jps.23926_bb0010) 1997; 14
Wang (10.1002/jps.23926_bb0130) 2010; 99
Searles (10.1002/jps.23926_bb0060) 2001; 90
Chieng (10.1002/jps.23926_bb0150) 2013; 85
Kasper (10.1002/jps.23926_bb0055) 2011; 78
Britt (10.1002/jps.23926_bb0265) 2012; 101
Chi (10.1002/jps.23926_bb0240) 2003; 20
Bee (10.1002/jps.23926_bb0275) 2011; 100
Khurana (10.1002/jps.23926_bb0195) 2001; 40
Angell (10.1002/jps.23926_bb0180) 1995; 267
Webb (10.1002/jps.23926_bb0100) 2003; 92
Kaminski (10.1002/jps.23926_bb0185) 2012; 9
Inoue (10.1002/jps.23926_bb0290) 2013; 88
Bhatnagar (10.1002/jps.23926_bb0115) 2007; 12
Vessely (10.1002/jps.23926_bb0260) 2005; 6
Chang (10.1002/jps.23926_bb0025) 2009; 98
Sun (10.1002/jps.23926_bb0295) 2012; 14
Zhu (10.1002/jps.23926_bb0165) 2011; 106
Manning (10.1002/jps.23926_bb0015) 1989; 6
Rathore (10.1002/jps.23926_bb0065) 2008; 24
Bantchev (10.1002/jps.23926_bb0245) 2003; 19
Speed (10.1002/jps.23926_bb0220) 1997; 6
Cochran (10.1002/jps.23926_bb0090) 2009; 98
Zuo (10.1002/jps.23926_bb0170) 2013; 9
References_xml – volume: 40
  start-page: 586
  year: 2001
  end-page: 595
  ident: bb0235
  article-title: Conformational origin of the aggregation of recombinant human factor VIII
  publication-title: Biochemistry
  contributor:
    fullname: Middaugh
– volume: 88
  start-page: 022601
  year: 2013
  ident: bb0175
  article-title: Deviations of the glass transition temperature in amorphous conjugated polymer thin films
  publication-title: Phys Rev E
  contributor:
    fullname: Wang
– volume: 63
  start-page: 166
  year: 1999
  end-page: 174
  ident: bb0070
  article-title: Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation
  publication-title: Biotechnol Bioeng
  contributor:
    fullname: Randolph
– volume: 10
  start-page: 1312
  year: 2001
  end-page: 1318
  ident: bb0210
  article-title: Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
  publication-title: Protein Sci
  contributor:
    fullname: Rischel
– volume: 7
  start-page: 1352
  year: 1998
  end-page: 1358
  ident: bb0215
  article-title: Thermodynamic characterization of an intermediate state of human growth hormone
  publication-title: Protein Sci
  contributor:
    fullname: Paton
– volume: 20
  start-page: 1325
  year: 2003
  end-page: 1336
  ident: bb0240
  article-title: Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
  publication-title: Pharm Res
  contributor:
    fullname: Carpenter
– volume: 16
  start-page: 249
  year: 1999
  end-page: 254
  ident: bb0125
  article-title: Protein inhalation powders: Spray drying vs spray freeze drying
  publication-title: Pharm Res
  contributor:
    fullname: Hsu
– volume: 4
  start-page: 754
  year: 2005
  end-page: 758
  ident: bb0280
  article-title: Residual stresses in thin polymer films cause rupture and dominate early stages of dewetting
  publication-title: Nat Mater
  contributor:
    fullname: Raphael
– volume: 3
  start-page: R9
  year: 1998
  end-page: R23
  ident: bb0200
  article-title: Protein aggregation: Folding aggregates, inclusion bodies and amyloid
  publication-title: Fold Des
  contributor:
    fullname: Fink
– volume: 90
  start-page: 872
  year: 2001
  end-page: 887
  ident: bb0060
  article-title: Annealing to optimize the primary drying rate, reduce freezing-induced drying rate heterogeneity, and determine
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 10
  start-page: 57
  year: 1996
  end-page: 66
  ident: bb0225
  article-title: Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates
  publication-title: FASEB J
  contributor:
    fullname: Mitraki
– volume: 9
  start-page: 1559
  year: 2012
  end-page: 1569
  ident: bb0185
  article-title: Dielectric studies on molecular dynamics of two important disaccharides: Sucrose and trehalose
  publication-title: Mol Pharm
  contributor:
    fullname: Tarnacka
– volume: 226
  start-page: 378
  year: 1996
  end-page: 384
  ident: bb0230
  article-title: Folding pathway of human alpha 1-antitrypsin: Characterization of an intermediate that is active but prone to aggregation
  publication-title: Biochem Biophys Res Commun
  contributor:
    fullname: Yu
– volume: 45
  start-page: 231
  year: 1998
  end-page: 238
  ident: bb0035
  article-title: Application of infrared spectroscopy to development of stable lyophilized protein formulations
  publication-title: Eur J Pharm Biopharm
  contributor:
    fullname: Dong
– volume: 12
  start-page: 505
  year: 2007
  end-page: 523
  ident: bb0115
  article-title: Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization
  publication-title: Pharm Dev Technol
  contributor:
    fullname: Pikal
– volume: 8
  start-page: 2983
  year: 2012
  end-page: 2991
  ident: bb0030
  article-title: beta-Relaxation governs protein stability in sugar–glass matrices
  publication-title: Soft Matter
  contributor:
    fullname: Douglas
– volume: 88
  start-page: 032601
  year: 2013
  ident: bb0290
  article-title: Distribution of glass transition temperature in multilayered poly(methyl methacrylate) thin film supported on a Si substrate as studied by neutron reflectivity
  publication-title: Phys Rev E
  contributor:
    fullname: Hino
– volume: 85
  start-page: 1325
  year: 1996
  end-page: 1330
  ident: bb0120
  article-title: Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
  publication-title: J Pharm Sci
  contributor:
    fullname: Carpenter
– volume: 86
  start-page: 1198
  year: 1997
  end-page: 1203
  ident: bb0040
  article-title: Phase separation of excipients during lyophilization: Effects on protein stability
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 78
  start-page: 248
  year: 2011
  end-page: 263
  ident: bb0055
  article-title: The freezing step in lyophilization: Physico-chemical fundamentals, freezing methods and consequences on process performance and quality attributes of biopharmaceuticals
  publication-title: Eur J Pharm Biopharm
  contributor:
    fullname: Friess
– volume: 188
  start-page: 243
  year: 1999
  end-page: 253
  ident: bb0160
  article-title: Spray-drying of trypsin—Surface characterisation and activity preservation
  publication-title: Int J Pharm
  contributor:
    fullname: Bergenstahl
– volume: 91
  start-page: 1474
  year: 2002
  end-page: 1487
  ident: bb0080
  article-title: Surface adsorption of recombinant human interferon-gamma in lyophilized and spray-lyophilized formulations
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 203
  start-page: 1
  year: 2000
  end-page: 60
  ident: bb0020
  article-title: Lyophilization and development of solid protein pharmaceuticals
  publication-title: Int J Pharm
  contributor:
    fullname: Wang
– volume: 15
  start-page: 16
  year: 2002
  end-page: 72
  ident: bb0110
  article-title: The importance of freezing on lyophilization cycle development
  publication-title: BioPharm
  contributor:
    fullname: Overcashier
– volume: 6
  start-page: 3334
  year: 2005
  end-page: 3344
  ident: bb0260
  article-title: Calcium-induced changes to the molecular conformation and aggregate structure of beta-casein at the air–water interface
  publication-title: Biomacromolecules
  contributor:
    fullname: Schwartz
– volume: 12
  start-page: 69
  year: 1995
  end-page: 77
  ident: bb0105
  article-title: Surface denaturation at solid–void interface—A possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen-activator at high-temperatures
  publication-title: Pharm Res
  contributor:
    fullname: Pearlman
– volume: 10
  start-page: 249
  year: 1982
  end-page: 259
  ident: bb0140
  article-title: Determination of residual moisture in freeze-dried viral vaccines—Fischer, Karl, gravimetric and thermogravimetric methodologies
  publication-title: J Biol Standard
  contributor:
    fullname: West
– volume: 44
  start-page: 3022
  year: 2006
  end-page: 3030
  ident: bb0285
  article-title: Viscoelastic dewetting of constrained polymer thin films
  publication-title: J Polym Sci B
  contributor:
    fullname: Raphael
– volume: 100
  start-page: 4158
  year: 2011
  end-page: 4170
  ident: bb0275
  article-title: Effects of surfaces and leachables on the stability of biopharmaceuticals
  publication-title: J Pharm Sci
  contributor:
    fullname: Dimitrova
– volume: 98
  start-page: 3495
  year: 2009
  end-page: 3498
  ident: bb0090
  article-title: Ice nucleation temperature influences recovery of activity of a model protein after freeze drying
  publication-title: J Pharm Sci
  contributor:
    fullname: Nail
– volume: 24
  start-page: 504
  year: 2008
  end-page: 514
  ident: bb0065
  article-title: Current perspectives on stability of protein drug products during formulation, fill and finish operations
  publication-title: Biotechnol Prog
  contributor:
    fullname: Rajan
– volume: 14
  start-page: 969
  year: 1997
  end-page: 975
  ident: bb0010
  article-title: Rational design of stable lyophilized protein formulations: Some practical advice
  publication-title: Pharm Res
  contributor:
    fullname: Randolph
– volume: 101
  start-page: 4419
  year: 2012
  end-page: 4432
  ident: bb0265
  article-title: Excipient effects on humanized monoclonal antibody interactions with silicone oil emulsions
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 85
  start-page: 197
  year: 2013
  end-page: 206
  ident: bb0150
  article-title: Characterization of dynamics in complex lyophilized formulations: II. Analysis of density variations in terms of glass dynamics and comparisons with global mobility, fast dynamics, and positron annihilation lifetime spectroscopy (PALS)
  publication-title: Eur J Pharm Biopharm
  contributor:
    fullname: Pikal
– volume: 90
  start-page: 860
  year: 2001
  end-page: 871
  ident: bb0075
  article-title: The ice nucleation temperature determines the primary drying rate of lyophilization for samples frozen on a temperature-controlled shelf
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 14
  start-page: 380
  year: 2012
  end-page: 388
  ident: bb0295
  article-title: Stability of amorphous pharmaceutical solids: Crystal growth mechanisms and effect of polymer additives
  publication-title: AAPS J
  contributor:
    fullname: Yu
– volume: 9
  start-page: 7855
  year: 2013
  end-page: 7865
  ident: bb0045
  article-title: Contributions of local mobility and degree of retention of native secondary structure to the stability of recombinant human growth hormone (rhGH) in glassy lyophilized formulations
  publication-title: Soft Matter
  contributor:
    fullname: Randolph
– volume: 5
  start-page: 54
  year: 2004
  end-page: 62
  ident: bb0095
  article-title: Heat and mass transfer scale-up issues during freeze drying: II. Control and characterization of the degree of supercooling
  publication-title: AAPS PharmSciTech
  contributor:
    fullname: Pikal
– volume: 17
  start-page: 863
  year: 2000
  end-page: 870
  ident: bb0155
  article-title: Surface composition of spray-dried particles of bovine serum albumin/trehalose/surfactant
  publication-title: Pharm Res
  contributor:
    fullname: Lee
– volume: 144
  start-page: 38
  year: 2008
  end-page: 53
  ident: bb0255
  article-title: Interfacial shear rheology of protein–surfactant layers
  publication-title: Adv Colloid Interface Sci
  contributor:
    fullname: Miller
– volume: 9
  start-page: 9376
  year: 2013
  end-page: 9384
  ident: bb0170
  article-title: Depth profile of the segmental dynamics at a poly(methyl methacrylate) film surface
  publication-title: Soft Matter
  contributor:
    fullname: Wang
– volume: 98
  start-page: 11
  year: 2009
  ident: bb0270
  article-title: Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation and accelerated stress stability studies
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 40
  start-page: 3525
  year: 2001
  end-page: 3535
  ident: bb0195
  article-title: Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
  publication-title: Biochemistry
  contributor:
    fullname: Fink
– volume: 6
  start-page: 903
  year: 1989
  end-page: 918
  ident: bb0015
  article-title: Stability of protein pharmaceuticals
  publication-title: Pharm Res
  contributor:
    fullname: Borchardt
– volume: 15
  start-page: 161
  year: 1999
  end-page: 176
  ident: bb0250
  article-title: Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
  publication-title: Colloids Surf B
  contributor:
    fullname: Dickinson
– volume: 33
  start-page: 12504
  year: 1994
  end-page: 12511
  ident: bb0205
  article-title: Classification of acid denaturation of proteins: Intermediates and unfolded states
  publication-title: Biochemistry
  contributor:
    fullname: Palleros
– volume: 97
  start-page: 163
  year: 2008
  end-page: 184
  ident: bb0050
  article-title: The impact of drying method and formulation on the physical properties and stability of methionyl human growth hormone in the amorphous solid state
  publication-title: J Pharm Sci
  contributor:
    fullname: Pikal
– volume: 92
  start-page: 715
  year: 2003
  end-page: 729
  ident: bb0100
  article-title: Effects of annealing lyophilized and spray-lyophilized formulations of recombinant human interferon-gamma
  publication-title: J Pharm Sci
  contributor:
    fullname: Randolph
– volume: 99
  start-page: 683
  year: 2010
  end-page: 700
  ident: bb0130
  article-title: The impact of thermal treatment on the stability of freeze-dried amorphous pharmaceuticals: II. Aggregation in an IgG1 fusion protein
  publication-title: J Pharm Sci
  contributor:
    fullname: Pikal
– volume: 106
  start-page: 256103
  year: 2011
  ident: bb0165
  article-title: Surface self-diffusion of an organic glass
  publication-title: Phys Rev Lett
  contributor:
    fullname: Yu
– volume: 6
  start-page: 99
  year: 1997
  end-page: 108
  ident: bb0220
  article-title: Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
  publication-title: Protein Sci
  contributor:
    fullname: King
– volume: 267
  start-page: 1924
  year: 1995
  end-page: 1935
  ident: bb0180
  article-title: Formation of glasses from liquids and biopolymers
  publication-title: Science
  contributor:
    fullname: Angell
– volume: 19
  start-page: 2673
  year: 2003
  end-page: 2682
  ident: bb0245
  article-title: Surface shear rheology of beta-casein layers at the air/solution interface: Formation of a two-dimensional physical gel
  publication-title: Langmuir
  contributor:
    fullname: Schwartz
– volume: 85
  start-page: 189
  year: 2013
  end-page: 196
  ident: bb0145
  article-title: Characterization of dynamics in complex lyophilized formulations: I. Comparison of relaxation times measured by isothermal calorimetry with data estimated from the width of the glass transition temperature region
  publication-title: Eur J Pharm Biopharm
  contributor:
    fullname: Pikal
– volume: 98
  start-page: 2886
  year: 2009
  end-page: 2908
  ident: bb0025
  article-title: Mechanisms of protein stabilization in the solid state
  publication-title: J Pharm Sci
  contributor:
    fullname: Pikal
– volume: 10
  start-page: 1406
  year: 2009
  end-page: 1411
  ident: bb0085
  article-title: Reduced pressure ice fog technique for controlled ice nucleation during freeze-drying
  publication-title: AAPS PharmSciTech
  contributor:
    fullname: Pikal
– volume: 107
  start-page: 663
  year: 2010
  end-page: 672
  ident: bb0135
  article-title: Crystallization of recombinant human growth hormone at elevated pressures: Pressure effects on PEG-induced volume exclusion interactions
  publication-title: Biotechnol Bioeng
  contributor:
    fullname: Randolph
– volume: 100
  start-page: 4631
  year: 2011
  end-page: 4641
  ident: bb0190
  article-title: Qualification of FTIR spectroscopic method for protein secondary structural analysis
  publication-title: J Pharm Sci
  contributor:
    fullname: Narhi
– volume: 8
  start-page: 2983
  issue: 10
  year: 2012
  end-page: 2991
  article-title: beta‐Relaxation governs protein stability in sugar–glass matrices
  publication-title: Soft Matter
– volume: 99
  start-page: 683
  issue: 2
  year: 2010
  end-page: 700
  article-title: The impact of thermal treatment on the stability of freeze‐dried amorphous pharmaceuticals: II. Aggregation in an g 1 fusion protein
  publication-title: J Pharm Sci
– volume: 6
  start-page: 99
  issue: 1
  year: 1997
  end-page: 108
  article-title: Conformation of 22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
  publication-title: Protein Sci
– volume: 144
  start-page: 38
  issue: 1–2
  year: 2008
  end-page: 53
  article-title: Interfacial shear rheology of protein–surfactant layers
  publication-title: Adv Colloid Interface Sci
– volume: 85
  start-page: 1325
  issue: 12
  year: 1996
  end-page: 1330
  article-title: Surface‐induced denaturation of proteins during freezing and its inhibition by surfactants
  publication-title: J Pharm Sci
– volume: 10
  start-page: 249
  issue: 3
  year: 1982
  end-page: 259
  article-title: Determination of residual moisture in freeze‐dried viral vaccines— ischer, arl, gravimetric and thermogravimetric methodologies
  publication-title: J Biol Standard
– volume: 6
  start-page: 903
  issue: 11
  year: 1989
  end-page: 918
  article-title: Stability of protein pharmaceuticals
  publication-title: Pharm Res
– volume: 88
  start-page: 032601
  issue: 3
  year: 2013
  article-title: Distribution of glass transition temperature in multilayered poly(methyl methacrylate) thin film supported on a i substrate as studied by neutron reflectivity
  publication-title: Phys Rev E
– volume: 14
  start-page: 380
  issue: 3
  year: 2012
  end-page: 388
  article-title: Stability of amorphous pharmaceutical solids: Crystal growth mechanisms and effect of polymer additives
  publication-title: AAPS J
– volume: 63
  start-page: 166
  issue: 2
  year: 1999
  end-page: 174
  article-title: Protein formulation and lyophilization cycle design: Prevention of damage due to freeze‐concentration induced phase separation
  publication-title: Biotechnol Bioeng
– volume: 90
  start-page: 860
  issue: 7
  year: 2001
  end-page: 871
  article-title: The ice nucleation temperature determines the primary drying rate of lyophilization for samples frozen on a temperature‐controlled shelf
  publication-title: J Pharm Sci
– volume: 78
  start-page: 248
  issue: 2
  year: 2011
  end-page: 263
  article-title: The freezing step in lyophilization: Physico‐chemical fundamentals, freezing methods and consequences on process performance and quality attributes of biopharmaceuticals
  publication-title: Eur J Pharm Biopharm
– volume: 20
  start-page: 1325
  issue: 9
  year: 2003
  end-page: 1336
  article-title: Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
  publication-title: Pharm Res
– volume: 45
  start-page: 231
  issue: 3
  year: 1998
  end-page: 238
  article-title: Application of infrared spectroscopy to development of stable lyophilized protein formulations
  publication-title: Eur J Pharm Biopharm
– volume: 40
  start-page: 586
  issue: 2
  year: 2001
  end-page: 595
  article-title: Conformational origin of the aggregation of recombinant human factor VIII
  publication-title: Biochemistry
– volume: 33
  start-page: 12504
  issue: 41
  year: 1994
  end-page: 12511
  article-title: Classification of acid denaturation of proteins: Intermediates and unfolded states
  publication-title: Biochemistry
– volume: 19
  start-page: 2673
  issue: 7
  year: 2003
  end-page: 2682
  article-title: Surface shear rheology of beta‐casein layers at the air/solution interface: Formation of a two‐dimensional physical gel
  publication-title: Langmuir
– volume: 100
  start-page: 4631
  issue: 11
  year: 2011
  end-page: 4641
  article-title: Qualification of spectroscopic method for protein secondary structural analysis
  publication-title: J Pharm Sci
– volume: 188
  start-page: 243
  issue: 2
  year: 1999
  end-page: 253
  article-title: Spray‐drying of trypsin—Surface characterisation and activity preservation
  publication-title: Int J Pharm
– volume: 17
  start-page: 863
  issue: 7
  year: 2000
  end-page: 870
  article-title: Surface composition of spray‐dried particles of bovine serum albumin/trehalose/surfactant
  publication-title: Pharm Res
– volume: 12
  start-page: 69
  issue: 1
  year: 1995
  end-page: 77
  article-title: Surface denaturation at solid–void interface—A possible pathway by which opalescent particulates form during the storage of lyophilized tissue‐type plasminogen‐activator at high‐temperatures
  publication-title: Pharm Res
– volume: 85
  start-page: 189
  issue: 2
  year: 2013
  end-page: 196
  article-title: Characterization of dynamics in complex lyophilized formulations: I. Comparison of relaxation times measured by isothermal calorimetry with data estimated from the width of the glass transition temperature region
  publication-title: Eur J Pharm Biopharm
– volume: 98
  start-page: 3495
  issue: 9
  year: 2009
  end-page: 3498
  article-title: Ice nucleation temperature influences recovery of activity of a model protein after freeze drying
  publication-title: J Pharm Sci
– volume: 9
  start-page: 9376
  issue: 39
  year: 2013
  end-page: 9384
  article-title: Depth profile of the segmental dynamics at a poly(methyl methacrylate) film surface
  publication-title: Soft Matter
– volume: 44
  start-page: 3022
  issue: 20
  year: 2006
  end-page: 3030
  article-title: Viscoelastic dewetting of constrained polymer thin films
  publication-title: J Polym Sci B
– volume: 9
  start-page: 7855
  issue: 32
  year: 2013
  end-page: 7865
  article-title: Contributions of local mobility and degree of retention of native secondary structure to the stability of recombinant human growth hormone (rh ) in glassy lyophilized formulations
  publication-title: Soft Matter
– volume: 10
  start-page: 1312
  issue: 7
  year: 2001
  end-page: 1318
  article-title: Conformational characterization of oligomeric intermediates and aggregates in beta‐lactoglobulin heat aggregation
  publication-title: Protein Sci
– volume: 97
  start-page: 163
  issue: 1
  year: 2008
  end-page: 184
  article-title: The impact of drying method and formulation on the physical properties and stability of methionyl human growth hormone in the amorphous solid state
  publication-title: J Pharm Sci
– volume: 16
  start-page: 249
  issue: 2
  year: 1999
  end-page: 254
  article-title: Protein inhalation powders: Spray drying vs spray freeze drying
  publication-title: Pharm Res
– volume: 100
  start-page: 4158
  issue: 10
  year: 2011
  end-page: 4170
  article-title: Effects of surfaces and leachables on the stability of biopharmaceuticals
  publication-title: J Pharm Sci
– volume: 40
  start-page: 3525
  issue: 12
  year: 2001
  end-page: 3535
  article-title: Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
  publication-title: Biochemistry
– volume: 98
  start-page: 11
  issue: 9
  year: 2009
  article-title: Monoclonal antibody interactions with micro‐ and nanoparticles: Adsorption, aggregation and accelerated stress stability studies
  publication-title: J Pharm Sci
– volume: 15
  start-page: 16
  issue: 3
  year: 2002
  end-page: 72
  article-title: The importance of freezing on lyophilization cycle development
  publication-title: BioPharm
– volume: 7
  start-page: 1352
  issue: 6
  year: 1998
  end-page: 1358
  article-title: Thermodynamic characterization of an intermediate state of human growth hormone
  publication-title: Protein Sci
– volume: 267
  start-page: 1924
  issue: 5206
  year: 1995
  end-page: 1935
  article-title: Formation of glasses from liquids and biopolymers
  publication-title: Science
– volume: 10
  start-page: 1406
  issue: 4
  year: 2009
  end-page: 1411
  article-title: Reduced pressure ice fog technique for controlled ice nucleation during freeze‐drying
  publication-title: AAPS PharmSciTech
– volume: 12
  start-page: 505
  issue: 5
  year: 2007
  end-page: 523
  article-title: Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization
  publication-title: Pharm Dev Technol
– volume: 107
  start-page: 663
  issue: 4
  year: 2010
  end-page: 672
  article-title: Crystallization of recombinant human growth hormone at elevated pressures: Pressure effects on ‐induced volume exclusion interactions
  publication-title: Biotechnol Bioeng
– volume: 88
  start-page: 022601
  issue: 2
  year: 2013
  article-title: Deviations of the glass transition temperature in amorphous conjugated polymer thin films
  publication-title: Phys Rev E
– volume: 14
  start-page: 969
  issue: 8
  year: 1997
  end-page: 975
  article-title: Rational design of stable lyophilized protein formulations: Some practical advice
  publication-title: Pharm Res
– volume: 5
  start-page: 54
  issue: 4
  year: 2004
  end-page: 62
  article-title: Heat and mass transfer scale‐up issues during freeze drying: II. Control and characterization of the degree of supercooling
  publication-title: AAPS PharmSciTech
– volume: 85
  start-page: 197
  issue: 2
  year: 2013
  end-page: 206
  article-title: Characterization of dynamics in complex lyophilized formulations: II. Analysis of density variations in terms of glass dynamics and comparisons with global mobility, fast dynamics, and positron annihilation lifetime spectroscopy ( )
  publication-title: Eur J Pharm Biopharm
– volume: 3
  start-page: R9
  issue: 1
  year: 1998
  end-page: R23
  article-title: Protein aggregation: Folding aggregates, inclusion bodies and amyloid
  publication-title: Fold Des
– volume: 6
  start-page: 3334
  issue: 6
  year: 2005
  end-page: 3344
  article-title: Calcium‐induced changes to the molecular conformation and aggregate structure of beta‐casein at the air–water interface
  publication-title: Biomacromolecules
– volume: 91
  start-page: 1474
  issue: 6
  year: 2002
  end-page: 1487
  article-title: Surface adsorption of recombinant human interferon‐gamma in lyophilized and spray‐lyophilized formulations
  publication-title: J Pharm Sci
– volume: 15
  start-page: 161
  year: 1999
  end-page: 176
  article-title: Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
  publication-title: Colloids Surf B
– volume: 24
  start-page: 504
  issue: 3
  year: 2008
  end-page: 514
  article-title: Current perspectives on stability of protein drug products during formulation, fill and finish operations
  publication-title: Biotechnol Prog
– volume: 90
  start-page: 872
  issue: 7
  year: 2001
  end-page: 887
  article-title: Annealing to optimize the primary drying rate, reduce freezing‐induced drying rate heterogeneity, and determine ′ in pharmaceutical lyophilization
  publication-title: J Pharm Sci
– volume: 106
  start-page: 256103
  issue: 25
  year: 2011
  article-title: Surface self‐diffusion of an organic glass
  publication-title: Phys Rev Lett
– volume: 203
  start-page: 1
  issue: 1–2
  year: 2000
  end-page: 60
  article-title: Lyophilization and development of solid protein pharmaceuticals
  publication-title: Int J Pharm
– volume: 86
  start-page: 1198
  issue: 11
  year: 1997
  end-page: 1203
  article-title: Phase separation of excipients during lyophilization: Effects on protein stability
  publication-title: J Pharm Sci
– volume: 10
  start-page: 57
  issue: 1
  year: 1996
  end-page: 66
  article-title: Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates
  publication-title: FASEB J
– volume: 226
  start-page: 378
  issue: 2
  year: 1996
  end-page: 384
  article-title: Folding pathway of human alpha 1‐antitrypsin: Characterization of an intermediate that is active but prone to aggregation
  publication-title: Biochem Biophys Res Commun
– volume: 98
  start-page: 2886
  issue: 9
  year: 2009
  end-page: 2908
  article-title: Mechanisms of protein stabilization in the solid state
  publication-title: J Pharm Sci
– volume: 101
  start-page: 4419
  issue: 12
  year: 2012
  end-page: 4432
  article-title: Excipient effects on humanized monoclonal antibody interactions with silicone oil emulsions
  publication-title: J Pharm Sci
– volume: 4
  start-page: 754
  issue: 10
  year: 2005
  end-page: 758
  article-title: Residual stresses in thin polymer films cause rupture and dominate early stages of dewetting
  publication-title: Nat Mater
– volume: 92
  start-page: 715
  issue: 4
  year: 2003
  end-page: 729
  article-title: Effects of annealing lyophilized and spray‐lyophilized formulations of recombinant human interferon‐gamma
  publication-title: J Pharm Sci
– volume: 9
  start-page: 1559
  issue: 6
  year: 2012
  end-page: 1569
  article-title: Dielectric studies on molecular dynamics of two important disaccharides: Sucrose and trehalose
  publication-title: Mol Pharm
– volume: 92
  start-page: 715
  issue: 4
  year: 2003
  ident: 10.1002/jps.23926_bb0100
  article-title: Effects of annealing lyophilized and spray-lyophilized formulations of recombinant human interferon-gamma
  publication-title: J Pharm Sci
  doi: 10.1002/jps.10334
  contributor:
    fullname: Webb
– volume: 40
  start-page: 586
  issue: 2
  year: 2001
  ident: 10.1002/jps.23926_bb0235
  article-title: Conformational origin of the aggregation of recombinant human factor VIII
  publication-title: Biochemistry
  doi: 10.1021/bi001547t
  contributor:
    fullname: Grillo
– volume: 63
  start-page: 166
  issue: 2
  year: 1999
  ident: 10.1002/jps.23926_bb0070
  article-title: Protein formulation and lyophilization cycle design: Prevention of damage due to freeze-concentration induced phase separation
  publication-title: Biotechnol Bioeng
  doi: 10.1002/(SICI)1097-0290(19990420)63:2<166::AID-BIT5>3.0.CO;2-H
  contributor:
    fullname: Heller
– volume: 107
  start-page: 663
  issue: 4
  year: 2010
  ident: 10.1002/jps.23926_bb0135
  article-title: Crystallization of recombinant human growth hormone at elevated pressures: Pressure effects on PEG-induced volume exclusion interactions
  publication-title: Biotechnol Bioeng
  doi: 10.1002/bit.22832
  contributor:
    fullname: Crisman
– volume: 267
  start-page: 1924
  issue: 5206
  year: 1995
  ident: 10.1002/jps.23926_bb0180
  article-title: Formation of glasses from liquids and biopolymers
  publication-title: Science
  doi: 10.1126/science.267.5206.1924
  contributor:
    fullname: Angell
– volume: 3
  start-page: R9
  issue: 1
  year: 1998
  ident: 10.1002/jps.23926_bb0200
  article-title: Protein aggregation: Folding aggregates, inclusion bodies and amyloid
  publication-title: Fold Des
  doi: 10.1016/S1359-0278(98)00002-9
  contributor:
    fullname: Fink
– volume: 98
  start-page: 11
  issue: 9
  year: 2009
  ident: 10.1002/jps.23926_bb0270
  article-title: Monoclonal antibody interactions with micro- and nanoparticles: Adsorption, aggregation and accelerated stress stability studies
  publication-title: J Pharm Sci
  doi: 10.1002/jps.21768
  contributor:
    fullname: Bee
– volume: 10
  start-page: 1406
  issue: 4
  year: 2009
  ident: 10.1002/jps.23926_bb0085
  article-title: Reduced pressure ice fog technique for controlled ice nucleation during freeze-drying
  publication-title: AAPS PharmSciTech
  doi: 10.1208/s12249-009-9338-7
  contributor:
    fullname: Patel
– volume: 100
  start-page: 4631
  issue: 11
  year: 2011
  ident: 10.1002/jps.23926_bb0190
  article-title: Qualification of FTIR spectroscopic method for protein secondary structural analysis
  publication-title: J Pharm Sci
  doi: 10.1002/jps.22686
  contributor:
    fullname: Jiang
– volume: 40
  start-page: 3525
  issue: 12
  year: 2001
  ident: 10.1002/jps.23926_bb0195
  article-title: Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
  publication-title: Biochemistry
  doi: 10.1021/bi001782b
  contributor:
    fullname: Khurana
– volume: 144
  start-page: 38
  issue: 1–2
  year: 2008
  ident: 10.1002/jps.23926_bb0255
  article-title: Interfacial shear rheology of protein–surfactant layers
  publication-title: Adv Colloid Interface Sci
  doi: 10.1016/j.cis.2008.08.010
  contributor:
    fullname: Krägel
– volume: 20
  start-page: 1325
  issue: 9
  year: 2003
  ident: 10.1002/jps.23926_bb0240
  article-title: Physical stability of proteins in aqueous solution: Mechanism and driving forces in nonnative protein aggregation
  publication-title: Pharm Res
  doi: 10.1023/A:1025771421906
  contributor:
    fullname: Chi
– volume: 106
  start-page: 256103
  issue: 25
  year: 2011
  ident: 10.1002/jps.23926_bb0165
  article-title: Surface self-diffusion of an organic glass
  publication-title: Phys Rev Lett
  doi: 10.1103/PhysRevLett.106.256103
  contributor:
    fullname: Zhu
– volume: 10
  start-page: 249
  issue: 3
  year: 1982
  ident: 10.1002/jps.23926_bb0140
  article-title: Determination of residual moisture in freeze-dried viral vaccines—Fischer, Karl, gravimetric and thermogravimetric methodologies
  publication-title: J Biol Standard
  doi: 10.1016/S0092-1157(82)80026-7
  contributor:
    fullname: May
– volume: 188
  start-page: 243
  issue: 2
  year: 1999
  ident: 10.1002/jps.23926_bb0160
  article-title: Spray-drying of trypsin—Surface characterisation and activity preservation
  publication-title: Int J Pharm
  doi: 10.1016/S0378-5173(99)00226-4
  contributor:
    fullname: Millqvist-Fureby
– volume: 6
  start-page: 99
  issue: 1
  year: 1997
  ident: 10.1002/jps.23926_bb0220
  article-title: Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
  publication-title: Protein Sci
  doi: 10.1002/pro.5560060111
  contributor:
    fullname: Speed
– volume: 17
  start-page: 863
  issue: 7
  year: 2000
  ident: 10.1002/jps.23926_bb0155
  article-title: Surface composition of spray-dried particles of bovine serum albumin/trehalose/surfactant
  publication-title: Pharm Res
  doi: 10.1023/A:1007568511399
  contributor:
    fullname: Adler
– volume: 101
  start-page: 4419
  issue: 12
  year: 2012
  ident: 10.1002/jps.23926_bb0265
  article-title: Excipient effects on humanized monoclonal antibody interactions with silicone oil emulsions
  publication-title: J Pharm Sci
  doi: 10.1002/jps.23318
  contributor:
    fullname: Britt
– volume: 86
  start-page: 1198
  issue: 11
  year: 1997
  ident: 10.1002/jps.23926_bb0040
  article-title: Phase separation of excipients during lyophilization: Effects on protein stability
  publication-title: J Pharm Sci
  doi: 10.1021/js970135b
  contributor:
    fullname: Randolph
– volume: 44
  start-page: 3022
  issue: 20
  year: 2006
  ident: 10.1002/jps.23926_bb0285
  article-title: Viscoelastic dewetting of constrained polymer thin films
  publication-title: J Polym Sci B
  doi: 10.1002/polb.20919
  contributor:
    fullname: Gabriele
– volume: 203
  start-page: 1
  issue: 1–2
  year: 2000
  ident: 10.1002/jps.23926_bb0020
  article-title: Lyophilization and development of solid protein pharmaceuticals
  publication-title: Int J Pharm
  doi: 10.1016/S0378-5173(00)00423-3
  contributor:
    fullname: Wang
– volume: 14
  start-page: 969
  issue: 8
  year: 1997
  ident: 10.1002/jps.23926_bb0010
  article-title: Rational design of stable lyophilized protein formulations: Some practical advice
  publication-title: Pharm Res
  doi: 10.1023/A:1012180707283
  contributor:
    fullname: Carpenter
– volume: 14
  start-page: 380
  issue: 3
  year: 2012
  ident: 10.1002/jps.23926_bb0295
  article-title: Stability of amorphous pharmaceutical solids: Crystal growth mechanisms and effect of polymer additives
  publication-title: AAPS J
  doi: 10.1208/s12248-012-9345-6
  contributor:
    fullname: Sun
– volume: 90
  start-page: 872
  issue: 7
  year: 2001
  ident: 10.1002/jps.23926_bb0060
  article-title: Annealing to optimize the primary drying rate, reduce freezing-induced drying rate heterogeneity, and determine Tg′ in pharmaceutical lyophilization
  publication-title: J Pharm Sci
  doi: 10.1002/jps.1040
  contributor:
    fullname: Searles
– volume: 15
  start-page: 16
  issue: 3
  year: 2002
  ident: 10.1002/jps.23926_bb0110
  article-title: The importance of freezing on lyophilization cycle development
  publication-title: BioPharm
  contributor:
    fullname: Patapoff
– volume: 85
  start-page: 1325
  issue: 12
  year: 1996
  ident: 10.1002/jps.23926_bb0120
  article-title: Surface-induced denaturation of proteins during freezing and its inhibition by surfactants
  publication-title: J Pharm Sci
  doi: 10.1021/js960080y
  contributor:
    fullname: Chang
– volume: 90
  start-page: 860
  issue: 7
  year: 2001
  ident: 10.1002/jps.23926_bb0075
  article-title: The ice nucleation temperature determines the primary drying rate of lyophilization for samples frozen on a temperature-controlled shelf
  publication-title: J Pharm Sci
  doi: 10.1002/jps.1039
  contributor:
    fullname: Searles
– volume: 91
  start-page: 1474
  issue: 6
  year: 2002
  ident: 10.1002/jps.23926_bb0080
  article-title: Surface adsorption of recombinant human interferon-gamma in lyophilized and spray-lyophilized formulations
  publication-title: J Pharm Sci
  doi: 10.1002/jps.10135
  contributor:
    fullname: Webb
– volume: 9
  start-page: 9376
  issue: 39
  year: 2013
  ident: 10.1002/jps.23926_bb0170
  article-title: Depth profile of the segmental dynamics at a poly(methyl methacrylate) film surface
  publication-title: Soft Matter
  doi: 10.1039/c3sm51658j
  contributor:
    fullname: Zuo
– volume: 226
  start-page: 378
  issue: 2
  year: 1996
  ident: 10.1002/jps.23926_bb0230
  article-title: Folding pathway of human alpha 1-antitrypsin: Characterization of an intermediate that is active but prone to aggregation
  publication-title: Biochem Biophys Res Commun
  doi: 10.1006/bbrc.1996.1364
  contributor:
    fullname: Kim
– volume: 24
  start-page: 504
  issue: 3
  year: 2008
  ident: 10.1002/jps.23926_bb0065
  article-title: Current perspectives on stability of protein drug products during formulation, fill and finish operations
  publication-title: Biotechnol Prog
  doi: 10.1021/bp070462h
  contributor:
    fullname: Rathore
– volume: 88
  start-page: 022601
  issue: 2
  year: 2013
  ident: 10.1002/jps.23926_bb0175
  article-title: Deviations of the glass transition temperature in amorphous conjugated polymer thin films
  publication-title: Phys Rev E
  doi: 10.1103/PhysRevE.88.022601
  contributor:
    fullname: Liu
– volume: 5
  start-page: 54
  issue: 4
  year: 2004
  ident: 10.1002/jps.23926_bb0095
  article-title: Heat and mass transfer scale-up issues during freeze drying: II. Control and characterization of the degree of supercooling
  publication-title: AAPS PharmSciTech
  doi: 10.1208/pt050458
  contributor:
    fullname: Rambhatla
– volume: 10
  start-page: 57
  issue: 1
  year: 1996
  ident: 10.1002/jps.23926_bb0225
  article-title: Thermolabile folding intermediates: Inclusion body precursors and chaperonin substrates
  publication-title: FASEB J
  doi: 10.1096/fasebj.10.1.8566549
  contributor:
    fullname: King
– volume: 12
  start-page: 505
  issue: 5
  year: 2007
  ident: 10.1002/jps.23926_bb0115
  article-title: Protein stability during freezing: Separation of stresses and mechanisms of protein stabilization
  publication-title: Pharm Dev Technol
  doi: 10.1080/10837450701481157
  contributor:
    fullname: Bhatnagar
– volume: 9
  start-page: 1559
  issue: 6
  year: 2012
  ident: 10.1002/jps.23926_bb0185
  article-title: Dielectric studies on molecular dynamics of two important disaccharides: Sucrose and trehalose
  publication-title: Mol Pharm
  doi: 10.1021/mp2004498
  contributor:
    fullname: Kaminski
– volume: 45
  start-page: 231
  issue: 3
  year: 1998
  ident: 10.1002/jps.23926_bb0035
  article-title: Application of infrared spectroscopy to development of stable lyophilized protein formulations
  publication-title: Eur J Pharm Biopharm
  doi: 10.1016/S0939-6411(98)00005-8
  contributor:
    fullname: Carpenter
– volume: 12
  start-page: 69
  issue: 1
  year: 1995
  ident: 10.1002/jps.23926_bb0105
  article-title: Surface denaturation at solid–void interface—A possible pathway by which opalescent particulates form during the storage of lyophilized tissue-type plasminogen-activator at high-temperatures
  publication-title: Pharm Res
  doi: 10.1023/A:1016270103863
  contributor:
    fullname: Hsu
– volume: 85
  start-page: 197
  issue: 2
  year: 2013
  ident: 10.1002/jps.23926_bb0150
  article-title: Characterization of dynamics in complex lyophilized formulations: II. Analysis of density variations in terms of glass dynamics and comparisons with global mobility, fast dynamics, and positron annihilation lifetime spectroscopy (PALS)
  publication-title: Eur J Pharm Biopharm
  doi: 10.1016/j.ejpb.2013.03.036
  contributor:
    fullname: Chieng
– volume: 78
  start-page: 248
  issue: 2
  year: 2011
  ident: 10.1002/jps.23926_bb0055
  article-title: The freezing step in lyophilization: Physico-chemical fundamentals, freezing methods and consequences on process performance and quality attributes of biopharmaceuticals
  publication-title: Eur J Pharm Biopharm
  doi: 10.1016/j.ejpb.2011.03.010
  contributor:
    fullname: Kasper
– volume: 16
  start-page: 249
  issue: 2
  year: 1999
  ident: 10.1002/jps.23926_bb0125
  article-title: Protein inhalation powders: Spray drying vs spray freeze drying
  publication-title: Pharm Res
  doi: 10.1023/A:1018828425184
  contributor:
    fullname: Maa
– volume: 33
  start-page: 12504
  issue: 41
  year: 1994
  ident: 10.1002/jps.23926_bb0205
  article-title: Classification of acid denaturation of proteins: Intermediates and unfolded states
  publication-title: Biochemistry
  doi: 10.1021/bi00207a018
  contributor:
    fullname: Fink
– volume: 19
  start-page: 2673
  issue: 7
  year: 2003
  ident: 10.1002/jps.23926_bb0245
  article-title: Surface shear rheology of beta-casein layers at the air/solution interface: Formation of a two-dimensional physical gel
  publication-title: Langmuir
  doi: 10.1021/la0262349
  contributor:
    fullname: Bantchev
– volume: 98
  start-page: 2886
  issue: 9
  year: 2009
  ident: 10.1002/jps.23926_bb0025
  article-title: Mechanisms of protein stabilization in the solid state
  publication-title: J Pharm Sci
  doi: 10.1002/jps.21825
  contributor:
    fullname: Chang
– volume: 97
  start-page: 163
  issue: 1
  year: 2008
  ident: 10.1002/jps.23926_bb0050
  article-title: The impact of drying method and formulation on the physical properties and stability of methionyl human growth hormone in the amorphous solid state
  publication-title: J Pharm Sci
  doi: 10.1002/jps.21085
  contributor:
    fullname: Abdul-Fattah
– volume: 100
  start-page: 4158
  issue: 10
  year: 2011
  ident: 10.1002/jps.23926_bb0275
  article-title: Effects of surfaces and leachables on the stability of biopharmaceuticals
  publication-title: J Pharm Sci
  doi: 10.1002/jps.22597
  contributor:
    fullname: Bee
– volume: 4
  start-page: 754
  issue: 10
  year: 2005
  ident: 10.1002/jps.23926_bb0280
  article-title: Residual stresses in thin polymer films cause rupture and dominate early stages of dewetting
  publication-title: Nat Mater
  doi: 10.1038/nmat1484
  contributor:
    fullname: Reiter
– volume: 8
  start-page: 2983
  issue: 10
  year: 2012
  ident: 10.1002/jps.23926_bb0030
  article-title: beta-Relaxation governs protein stability in sugar–glass matrices
  publication-title: Soft Matter
  doi: 10.1039/c2sm06979b
  contributor:
    fullname: Cicerone
– volume: 88
  start-page: 032601
  issue: 3
  year: 2013
  ident: 10.1002/jps.23926_bb0290
  article-title: Distribution of glass transition temperature in multilayered poly(methyl methacrylate) thin film supported on a Si substrate as studied by neutron reflectivity
  publication-title: Phys Rev E
  doi: 10.1103/PhysRevE.88.032601
  contributor:
    fullname: Inoue
– volume: 98
  start-page: 3495
  issue: 9
  year: 2009
  ident: 10.1002/jps.23926_bb0090
  article-title: Ice nucleation temperature influences recovery of activity of a model protein after freeze drying
  publication-title: J Pharm Sci
  doi: 10.1002/jps.21815
  contributor:
    fullname: Cochran
– volume: 15
  start-page: 161
  year: 1999
  ident: 10.1002/jps.23926_bb0250
  article-title: Adsorbed protein layers at fluid interfaces: Interactions, structure and surface rheology
  publication-title: Colloids Surf B
  doi: 10.1016/S0927-7765(99)00042-9
  contributor:
    fullname: Dickinson
– volume: 10
  start-page: 1312
  issue: 7
  year: 2001
  ident: 10.1002/jps.23926_bb0210
  article-title: Conformational characterization of oligomeric intermediates and aggregates in beta-lactoglobulin heat aggregation
  publication-title: Protein Sci
  doi: 10.1110/ps.42501
  contributor:
    fullname: Carrotta
– volume: 7
  start-page: 1352
  issue: 6
  year: 1998
  ident: 10.1002/jps.23926_bb0215
  article-title: Thermodynamic characterization of an intermediate state of human growth hormone
  publication-title: Protein Sci
  doi: 10.1002/pro.5560070611
  contributor:
    fullname: Gomez-Orellana
– volume: 6
  start-page: 3334
  issue: 6
  year: 2005
  ident: 10.1002/jps.23926_bb0260
  article-title: Calcium-induced changes to the molecular conformation and aggregate structure of beta-casein at the air–water interface
  publication-title: Biomacromolecules
  doi: 10.1021/bm050353w
  contributor:
    fullname: Vessely
– volume: 6
  start-page: 903
  issue: 11
  year: 1989
  ident: 10.1002/jps.23926_bb0015
  article-title: Stability of protein pharmaceuticals
  publication-title: Pharm Res
  doi: 10.1023/A:1015929109894
  contributor:
    fullname: Manning
– volume: 99
  start-page: 683
  issue: 2
  year: 2010
  ident: 10.1002/jps.23926_bb0130
  article-title: The impact of thermal treatment on the stability of freeze-dried amorphous pharmaceuticals: II. Aggregation in an IgG1 fusion protein
  publication-title: J Pharm Sci
  doi: 10.1002/jps.21960
  contributor:
    fullname: Wang
– volume: 85
  start-page: 189
  issue: 2
  year: 2013
  ident: 10.1002/jps.23926_bb0145
  article-title: Characterization of dynamics in complex lyophilized formulations: I. Comparison of relaxation times measured by isothermal calorimetry with data estimated from the width of the glass transition temperature region
  publication-title: Eur J Pharm Biopharm
  doi: 10.1016/j.ejpb.2013.04.003
  contributor:
    fullname: Chieng
– volume: 9
  start-page: 7855
  issue: 32
  year: 2013
  ident: 10.1002/jps.23926_bb0045
  article-title: Contributions of local mobility and degree of retention of native secondary structure to the stability of recombinant human growth hormone (rhGH) in glassy lyophilized formulations
  publication-title: Soft Matter
  doi: 10.1039/c3sm51251g
  contributor:
    fullname: Xu
SSID ssj0006055
Score 2.3572054
Snippet Recombinant human growth hormone (rhGH) was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and...
Recombinant human growth hormone (rhGH) was lyophilized with various glass‐forming stabilizers, employing cycles that incorporated various freezing and...
rhGH was lyophilized with various glass-forming stabilizers, employing cycles that incorporated various freezing and annealing procedures to manipulate glass...
SourceID pubmedcentral
proquest
crossref
pubmed
wiley
elsevier
SourceType Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 1356
SubjectTerms annealing
Chemistry, Pharmaceutical - methods
Circular Dichroism - methods
Drug Stability
Freeze Drying - methods
Glass - chemistry
growth hormone
Human Growth Hormone - chemistry
Humans
lyophilization
mobility
Powders - chemistry
protein formulation
protein structure
Protein Structure, Secondary
Recombinant Proteins - chemistry
specific surface area
stability
surface degradation
Transition Temperature
Water - chemistry
Title Protein Quantity on the Air–Solid Interface Determines Degradation Rates of Human Growth Hormone in Lyophilized Samples
URI https://dx.doi.org/10.1002/jps.23926
https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fjps.23926
https://www.ncbi.nlm.nih.gov/pubmed/24623139
https://www.proquest.com/docview/1511956834
https://search.proquest.com/docview/1513052139
https://pubmed.ncbi.nlm.nih.gov/PMC4049081
Volume 103
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELaqnrjwfoQWZBCqOGy2jWPHiThVlLKqAC3dVuoBKbIdm25ByWqzK5Se-A_9h_0ljO0kSymVEDdLdh62Z-xvPDOfEXolLIlTplkoAQ-ENOI6FFKZMNIFkSYWTBU2G_njp2R0TA9O2MkaetPlwnh-iP7AzWqGW6-tggtZb69IQ89m9ZDA7m7ptqOY23CuvcMVdRTAdNYzhYMR1LEK7ZDt_smb9qLrWPN6yOTvUNbtRft30JeuFz4E5dtwuZBDdf4HweN_dvMuut1iVLzrheoeWtPlfbQ19iTXzQAfrXK26gHewuMV_XXzADVjS_0wLfHnpbA5wA2uSgwwE-9O55c_LybV92mB3UGkEUrjvTYeR9dQ_DoX_o4nfGgxMK4Mdl4G_H5e_Vic4hEg7KrUGN7-oalm9jDoXBd4IizHcf0QHe-_O3o7CtsLHkIFdlISGiKMZowonRqRmSIykiSFyFLGJeU8lYqwmEueAK5RkeCJ0DsKFhFJC5mCYRc_QuslfPUJwgBVIlUYxnUBGIskYJiZjEaEG0G1TkyAXnZTnc88j0fuGZtJDkOcuyEO0KATgrwFIB5Y5DAvf2u-2QlK3mp-nUfWMcuSNKYBetFXg85aR4wodbV0bWKbNB1nAXrs5ar_KUIBkLoafkXi-gaWD_xqTTk9dbzg1HlxowC9dgJ1cz_zg_HEFZ7-e9MNdAuwIvWxnptofTFf6meAxxbyuVO8Xy-vNh4
link.rule.ids 230,315,783,787,888,1378,27937,27938,46307,46731
linkProvider Wiley-Blackwell
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VcoAL70eggEGo4rDZNs5rI3GpKGUp22rpbqVeqsh2bLotSlabXaH0xH_gH_JLGNtJllIqIW6WPHnYnrE_z3g-A7xmmsQpkaHLEQ-4gRdLl3GhXE9mlCufhSLT2ch7-1H_MNg9Co9W4G2TC2P5IVqHm7YMM19rA9cO6Y0la-jptOxSXN6ja3Adzd3XZrl9sCSPQqAetlzhuA1qeIU26Ub76FWr0WW0efnQ5O9g1qxGO7fhuGmHPYRy1l3MeVec_0Hx-L8NvQO3aphKtqxe3YUVmd-D9aHlua46ZLxM2yo7ZJ0MlwzY1X2ohpr9YZKTzwum04ArUuQEkSbZmsx-fv8xKr5OMmJ8kYoJSbbrIzmyxOKXGbPXPJEDDYNJoYgJNJAPs-Lb_IT0EWQXuST49kFVTLU_6FxmZMQ0zXH5AA533o_f9d36jgdX4FYpchVlSoYhFbKnWKIyT3EaZSzphTEP4rjHBQ39mMcRQhvhsThiclPgPMKDjPdwb-c_hNUcv_oYCKIVT2QqjGWGMItGuDdTSeDRWLFAykg58KoZ63RqqTxSS9pMU-zi1HSxA51GC9Iag1hskeLA_E18rdGUtDb-MvV0bDaMen7gwMu2Gs1Wx2JYLouFkfF13rSfOPDIKlb7UzRATGpq4gsq1wpoSvCLNfnkxFCDByaQ6znwxmjU1e1Md4cjU3jy76Iv4EZ_vDdIBx_3Pz2FmwgdA3v0cw1W57OFfIbwbM6fGyv8BVM4Ojc
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnZ1Jb9QwFMetUiTEhX0JFDAIVRwm08axs4hTRRmGUqqh00o9IFm2Y7dTUDKazAilJ74D35BPwrOzDKVUQtws2VnsvGf_vLx_EHoprIhTqpkvgQd8GsTaF1IZP9AZkSYUTGU2GvnjXjQ8pDtH7GgFvW5jYWp9iG7BzXqG66-tg08zs7EUDT2dln0Co3t0BV2lEZiqJaL9pXYUcDrrpMJhFtTKCm2Sje7Sywaji7B58czk7yzrBqPBTfS5rUZ9BuVLfzGXfXX2h8Ljf9bzFrrRQCreqq3qNlrR-R20PqpVrqsePlgGbZU9vI5HS_3r6i6qRlb7YZLjTwthg4ArXOQYOBNvTWY_v_8YF18nGXYrkUYojbebAzm6hOTxTNQ_ecL7FoJxYbDbZsDvZsW3-QkeAmIXucZw992qmNrVoDOd4bGwIsflPXQ4eHvwZug3f3jwFUyUIt8QYTRjROnEiNRkgZEkykSasFjSOE6kIiyMZRwB2KhAxJHQmwp6EUkzmcDMLryPVnN46kOEgVUClRkW6wwgi0QwMzMpDUhsBNU6Mh560X5qPq2FPHgt2Uw4NDF3TeyhXmsEvCGQmiw4fJe_FV9rDYU3rl_ywO7MsigJqYeed9ngtHYnRuS6WLgyoY2aDlMPPajtqnspQoFIXU58zuK6AlYQ_HxOPjlxwuDUbeMGHnrlDOryevKd0dglHv170Wfo2mh7wHff7314jK4DN9L63OcaWp3PFvoJsNlcPnU--AuJRDjm
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Protein+Quantity+on+the+Air%E2%80%93Solid+Interface+Determines+Degradation+Rates+of+Human+Growth+Hormone+in+Lyophilized+Samples&rft.jtitle=Journal+of+pharmaceutical+sciences&rft.au=Xu%2C+Yemin&rft.au=Grobelny%2C+Pawel&rft.au=Von+Allmen%2C+Alexander&rft.au=Knudson%2C+Korben&rft.date=2014-05-01&rft.pub=Elsevier+Inc&rft.issn=0022-3549&rft.eissn=1520-6017&rft.volume=103&rft.issue=5&rft.spage=1356&rft.epage=1366&rft_id=info:doi/10.1002%2Fjps.23926&rft.externalDocID=S0022354915305992
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0022-3549&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0022-3549&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0022-3549&client=summon