Protein stabilization by cyclodextrins in the liquid and dried state

Aggregation is arguably the biggest challenge for the development of stable formulations and robust manufacturing processes of therapeutic proteins. In search of novel excipients inhibiting protein aggregation, cyclodextrins and their derivatives have been under examination for use in parenteral pro...

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Published inAdvanced drug delivery reviews Vol. 63; no. 13; pp. 1086 - 1106
Main Authors Serno, Tim, Geidobler, Raimund, Winter, Gerhard
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.10.2011
Subjects
Animals
Cavities
Cyclodextrin
Cyclodextrins - chemistry
Drug Design
Drug Stability
Excipients - chemistry
HPβCD
Humans
Hydrophobic and Hydrophilic Interactions
Injections
Liquid formulation
Lyophilization
Monoclonal antibody
Non-ionic surfactant
Protein
Protein aggregation
Protein formulation
Protein stabilization
Proteins - administration & dosage
Proteins - chemistry
Cyclodextrin
Protein aggregation
Non-ionic surfactant
HPβCD
Liquid formulation
Lyophilization
Monoclonal antibody
Protein formulation
Protein
Protein stabilization
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Abstract Aggregation is arguably the biggest challenge for the development of stable formulations and robust manufacturing processes of therapeutic proteins. In search of novel excipients inhibiting protein aggregation, cyclodextrins and their derivatives have been under examination for use in parenteral protein products since more than 20 years and significant research work has been accomplished highlighting the great potential of cyclodextrins as stabilizers of therapeutic proteins. Oftentimes, the potential of cyclodextrins to inhibit protein aggregation has been attributed to their capability to incorporate hydrophobic residues on aggregation-prone proteins or on their partially unfolded intermediates into the hydrophobic cavity. In addition, also other mechanisms besides or even instead of complex formation play a role in the stabilization mechanism, e.g. non-ionic surfactant-like effects. In this review a comprehensive overview of the available research work on the beneficial use of cyclodextrins and their derivatives in protein formulations, liquid as well as dried, is provided. The mechanisms of stabilization against different kinds of stress conditions, such as thermal or surface-induced, are discussed in detail. [Display omitted]
AbstractList Aggregation is arguably the biggest challenge for the development of stable formulations and robust manufacturing processes of therapeutic proteins. In search of novel excipients inhibiting protein aggregation, cyclodextrins and their derivatives have been under examination for use in parenteral protein products since more than 20 years and significant research work has been accomplished highlighting the great potential of cyclodextrins as stabilizers of therapeutic proteins. Oftentimes, the potential of cyclodextrins to inhibit protein aggregation has been attributed to their capability to incorporate hydrophobic residues on aggregation-prone proteins or on their partially unfolded intermediates into the hydrophobic cavity. In addition, also other mechanisms besides or even instead of complex formation play a role in the stabilization mechanism, e.g. non-ionic surfactant-like effects. In this review a comprehensive overview of the available research work on the beneficial use of cyclodextrins and their derivatives in protein formulations, liquid as well as dried, is provided. The mechanisms of stabilization against different kinds of stress conditions, such as thermal or surface-induced, are discussed in detail.
Aggregation is arguably the biggest challenge for the development of stable formulations and robust manufacturing processes of therapeutic proteins. In search of novel excipients inhibiting protein aggregation, cyclodextrins and their derivatives have been under examination for use in parenteral protein products since more than 20 years and significant research work has been accomplished highlighting the great potential of cyclodextrins as stabilizers of therapeutic proteins. Oftentimes, the potential of cyclodextrins to inhibit protein aggregation has been attributed to their capability to incorporate hydrophobic residues on aggregation-prone proteins or on their partially unfolded intermediates into the hydrophobic cavity. In addition, also other mechanisms besides or even instead of complex formation play a role in the stabilization mechanism, e.g. non-ionic surfactant-like effects. In this review a comprehensive overview of the available research work on the beneficial use of cyclodextrins and their derivatives in protein formulations, liquid as well as dried, is provided. The mechanisms of stabilization against different kinds of stress conditions, such as thermal or surface-induced, are discussed in detail. [Display omitted]
Author Winter, Gerhard
Geidobler, Raimund
Serno, Tim
Author_xml – sequence: 1
  givenname: Tim
  surname: Serno
  fullname: Serno, Tim
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  organization: Novartis Pharma AG, Biologics Process R&D, Pharmaceutical Development, 4056 Basel, Switzerland
– sequence: 2
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  surname: Geidobler
  fullname: Geidobler, Raimund
  organization: Department of Pharmacy, Ludwig-Maximilians-University, 81377 Munich, Germany
– sequence: 3
  givenname: Gerhard
  surname: Winter
  fullname: Winter, Gerhard
  organization: Department of Pharmacy, Ludwig-Maximilians-University, 81377 Munich, Germany
BackLink https://www.ncbi.nlm.nih.gov/pubmed/21907254$$D View this record in MEDLINE/PubMed
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Issue 13
Keywords Cyclodextrin
Protein aggregation
Non-ionic surfactant
HPβCD
Liquid formulation
Lyophilization
Monoclonal antibody
Protein formulation
Protein
Protein stabilization
Language English
License Copyright © 2011 Elsevier B.V. All rights reserved.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c453t-d8e862981f017d08bee1e0662c13b3c9e0d333f43c4bcf19ca879a66896dddf83
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ObjectType-Feature-1
PMID 21907254
PQID 900629690
PQPubID 23479
PageCount 21
ParticipantIDs proquest_miscellaneous_904495452
proquest_miscellaneous_900629690
crossref_primary_10_1016_j_addr_2011_08_003
pubmed_primary_21907254
elsevier_sciencedirect_doi_10_1016_j_addr_2011_08_003
PublicationCentury 2000
PublicationDate 2011-10-01
PublicationDateYYYYMMDD 2011-10-01
PublicationDate_xml – month: 10
  year: 2011
  text: 2011-10-01
  day: 01
PublicationDecade 2010
PublicationPlace Netherlands
PublicationPlace_xml – name: Netherlands
PublicationTitle Advanced drug delivery reviews
PublicationTitleAlternate Adv Drug Deliv Rev
PublicationYear 2011
Publisher Elsevier B.V
Publisher_xml – name: Elsevier B.V
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Snippet Aggregation is arguably the biggest challenge for the development of stable formulations and robust manufacturing processes of therapeutic proteins. In search...
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SubjectTerms Animals
Cavities
Cyclodextrin
Cyclodextrins - chemistry
Drug Design
Drug Stability
Excipients - chemistry
HPβCD
Humans
Hydrophobic and Hydrophilic Interactions
Injections
Liquid formulation
Lyophilization
Monoclonal antibody
Non-ionic surfactant
Protein
Protein aggregation
Protein formulation
Protein stabilization
Proteins - administration & dosage
Proteins - chemistry
Title Protein stabilization by cyclodextrins in the liquid and dried state
URI https://dx.doi.org/10.1016/j.addr.2011.08.003
https://www.ncbi.nlm.nih.gov/pubmed/21907254
https://search.proquest.com/docview/900629690
https://search.proquest.com/docview/904495452
Volume 63
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