How Do Phenolic Acids Change the Secondary and Tertiary Structure of Gliadin? Studies with an Application of Spectroscopic Techniques

The effect of the chemical structure of selected phenolic acids on the molecular organization of gliadins was investigated with the application of Fourier Transform Infrared (FTIR) technique, steady-state, and time-resolved fluorescence spectroscopy. Hydroxybenzoic (4-hydroxybenzoic, protocatechuic,...

Full description

Saved in:
Bibliographic Details
Published inInternational journal of molecular sciences Vol. 23; no. 11; p. 6053
Main Authors Welc, Renata, Luchowski, Rafał, Kłosok, Konrad, Gruszecki, Wiesław I, Nawrocka, Agnieszka
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 27.05.2022
MDPI
Subjects
Amino acids
Chains
Disaggregation
Fluorescence spectroscopy
Fourier transforms
FTIR technique
Gliadin
Gluten
Hydrocarbons
Hydrogen bonds
Hydrophobicity
Hydroxycinnamic acid
Lifetime
Molecular weight
Phenolic acids
Polypeptides
Polyphenols
Protein structure
Proteins
secondary structure
Spectrum analysis
Stiffness
Tertiary structure
time-resolved fluorescence
secondary structure
time-resolved fluorescence
FTIR technique
gliadin
phenolic acids
Online AccessGet full text

Cover

Abstract The effect of the chemical structure of selected phenolic acids on the molecular organization of gliadins was investigated with the application of Fourier Transform Infrared (FTIR) technique, steady-state, and time-resolved fluorescence spectroscopy. Hydroxybenzoic (4-hydroxybenzoic, protocatechuic, vanillic, and syringic) and hydroxycinnamic (coumaric, caffeic, ferulic, sinapic) acids have been used as gliadins modifiers. The results indicated that hydroxybenzoic acids due to their smaller size incorporate into spaces between two polypeptide chains and form a hydrogen bond with them leading to aggregation. Additionally, syringic acids could incorporate into hydrophobic pockets of protein. Whereas hydroxycinnamic acids, due to their higher stiffness and larger size, separated polypeptide chains leading to gliadin disaggregation. These acids did not incorporate into hydrophobic pockets.
AbstractList The effect of the chemical structure of selected phenolic acids on the molecular organization of gliadins was investigated with the application of Fourier Transform Infrared (FTIR) technique, steady-state, and time-resolved fluorescence spectroscopy. Hydroxybenzoic (4-hydroxybenzoic, protocatechuic, vanillic, and syringic) and hydroxycinnamic (coumaric, caffeic, ferulic, sinapic) acids have been used as gliadins modifiers. The results indicated that hydroxybenzoic acids due to their smaller size incorporate into spaces between two polypeptide chains and form a hydrogen bond with them leading to aggregation. Additionally, syringic acids could incorporate into hydrophobic pockets of protein. Whereas hydroxycinnamic acids, due to their higher stiffness and larger size, separated polypeptide chains leading to gliadin disaggregation. These acids did not incorporate into hydrophobic pockets.
Author Nawrocka, Agnieszka
Kłosok, Konrad
Welc, Renata
Gruszecki, Wiesław I
Luchowski, Rafał
AuthorAffiliation 2 Department of Biophysics, Institute of Physics, Maria Curie Skłodowska University, 20-031 Lublin, Poland; rafal.luchowski@mail.umcs.pl (R.L.); wieslaw.gruszecki@mail.umcs.pl (W.I.G.)
1 Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland; k.klosok@ipan.lublin.pl (K.K.); a.nawrocka@ipan.lublin.pl (A.N.)
AuthorAffiliation_xml – name: 2 Department of Biophysics, Institute of Physics, Maria Curie Skłodowska University, 20-031 Lublin, Poland; rafal.luchowski@mail.umcs.pl (R.L.); wieslaw.gruszecki@mail.umcs.pl (W.I.G.)
– name: 1 Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland; k.klosok@ipan.lublin.pl (K.K.); a.nawrocka@ipan.lublin.pl (A.N.)
Author_xml – sequence: 1
  givenname: Renata
  orcidid: 0000-0003-0784-898X
  surname: Welc
  fullname: Welc, Renata
  organization: Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
– sequence: 2
  givenname: Rafał
  surname: Luchowski
  fullname: Luchowski, Rafał
  organization: Department of Biophysics, Institute of Physics, Maria Curie Skłodowska University, 20-031 Lublin, Poland
– sequence: 3
  givenname: Konrad
  orcidid: 0000-0001-7712-0041
  surname: Kłosok
  fullname: Kłosok, Konrad
  organization: Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
– sequence: 4
  givenname: Wiesław I
  surname: Gruszecki
  fullname: Gruszecki, Wiesław I
  organization: Department of Biophysics, Institute of Physics, Maria Curie Skłodowska University, 20-031 Lublin, Poland
– sequence: 5
  givenname: Agnieszka
  orcidid: 0000-0001-8618-2092
  surname: Nawrocka
  fullname: Nawrocka, Agnieszka
  organization: Institute of Agrophysics, Polish Academy of Sciences, Doświadczalna 4, 20-290 Lublin, Poland
BackLink https://www.ncbi.nlm.nih.gov/pubmed/35682729$$D View this record in MEDLINE/PubMed
BookMark eNpdkk9v0zAYhy00xLbCjTOyxIUDBf9JnPjCVBXYJk0Cqb1bjv2mcZXawU6Y-AB8bxw6po6T7dePHvv96b1EZz54QOg1JR84l-Sj2x8S45QKUvJn6IIWjC0JEdXZyf4cXaa0J4RxVsoX6JyXomYVkxfo9024x58D_t6BD70zeGWcTXjdab8DPHaAN2CCtzr-wtpbvIU4uvmwGeNkxikCDi2-7p22zl_l6mQdJHzvxi7zeDUMWapHF_zMbQYwYwzJhCE_tQXTefdjgvQSPW91n-DVw7pA269ftuub5d2369v16m5puOR8STXISlbENrTktrZaSEIpJ3kxjIsaSsat0YVsKBGkqqAlRUMkqyxnxFi-QLdHrQ16r4boDrkTFbRTfwsh7pTO7ZkeVNNQUWoqaqObgjZEQ62FAVOWpdVWtNn16egapuYA1oAfo-6fSJ_eeNepXfipJK0prWQWvHsQxDBnMKqDSwb6XnsIU1JMVKWghBOa0bf_ofswRZ-TmqmCC1LkeBbo_ZEyOeEUoX38DCVqHhV1OioZf3PawCP8bzb4H642vNo
CitedBy_id crossref_primary_10_1016_j_jcs_2024_103915
crossref_primary_10_1016_j_apt_2024_104459
crossref_primary_10_1016_j_jcs_2023_103682
crossref_primary_10_1039_D2FO02576K
crossref_primary_10_3390_molecules28237790
crossref_primary_10_1016_j_foodhyd_2023_109522
crossref_primary_10_3390_nano14121022
Cites_doi 10.3390/molecules26020508
10.1039/C8FO01997E
10.1016/j.bcp.2017.04.004
10.1016/j.foodchem.2013.05.136
10.1016/j.foodchem.2017.03.117
10.1038/s41598-017-09941-4
10.1074/jbc.M113.464222
10.1007/978-1-4757-3061-6
10.1207/s15327914nc5602_9
10.1002/anie.201713416
10.1002/jrs.4288
10.1002/psc.1085
10.1016/j.foodchem.2012.06.114
10.1016/j.foodchem.2011.09.047
10.1016/j.jconrel.2012.04.036
10.1016/j.foodchem.2011.05.084
10.1016/j.foodchem.2011.01.079
10.1007/s10895-013-1277-8
10.1021/jf049061x
10.1021/acs.jafc.5b05712
10.1016/j.jep.2012.06.022
10.1016/j.saa.2019.117937
10.1021/bi2015162
10.1016/j.cis.2019.05.002
10.1016/j.aninu.2020.01.001
10.1111/j.1749-6632.1973.tb47526.x
10.1016/j.foodchem.2018.01.110
ContentType Journal Article
Copyright 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
2022 by the authors. 2022
Copyright_xml – notice: 2022 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
– notice: 2022 by the authors. 2022
DBID NPM
AAYXX
CITATION
3V.
7X7
7XB
88E
8FI
8FJ
8FK
8G5
ABUWG
AFKRA
AZQEC
BENPR
CCPQU
DWQXO
FYUFA
GHDGH
GNUQQ
GUQSH
K9.
M0S
M1P
M2O
MBDVC
PIMPY
PQEST
PQQKQ
PQUKI
PRINS
Q9U
7X8
5PM
DOA
DOI 10.3390/ijms23116053
DatabaseName PubMed
CrossRef
ProQuest Central (Corporate)
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
Research Library (Alumni Edition)
ProQuest Central (Alumni)
ProQuest Central
ProQuest Central Essentials
ProQuest Central
ProQuest One Community College
ProQuest Central
Health Research Premium Collection
Health Research Premium Collection (Alumni)
ProQuest Central Student
Research Library Prep
ProQuest Health & Medical Complete (Alumni)
Health & Medical Collection (Alumni Edition)
PML(ProQuest Medical Library)
ProQuest research library
Research Library (Corporate)
Publicly Available Content Database
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
ProQuest Central China
ProQuest Central Basic
MEDLINE - Academic
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle PubMed
CrossRef
Publicly Available Content Database
Research Library Prep
ProQuest Central Student
ProQuest Central Essentials
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
Research Library (Alumni Edition)
ProQuest Central China
ProQuest Central
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
ProQuest Research Library
ProQuest Medical Library (Alumni)
ProQuest Central Basic
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
ProQuest Hospital Collection (Alumni)
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
ProQuest One Academic
ProQuest Central (Alumni)
MEDLINE - Academic
DatabaseTitleList PubMed


CrossRef
Publicly Available Content Database
Database_xml – sequence: 1
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  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: 3
  dbid: BENPR
  name: ProQuest Central
  url: https://www.proquest.com/central
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1422-0067
ExternalDocumentID oai_doaj_org_article_bb165a168cab41b0ae8a6cec555dad6f
10_3390_ijms23116053
35682729
Genre Journal Article
GrantInformation_xml – fundername: Polish Academy of Sciences
  grantid: OPUS 18 2019/35/B/NZ9/02854
– fundername: the National Science Centre, Poland
  grantid: 2019/35/B/NZ9/02854
GroupedDBID ---
29J
2WC
3V.
53G
5GY
5VS
7X7
88E
8FE
8FG
8FH
8FI
8FJ
8G5
A8Z
AADQD
AAFWJ
AAHBH
ABDBF
ABJCF
ABUWG
ACGFO
ACIHN
ACIWK
ACPRK
ADBBV
AEAQA
AENEX
AFKRA
AFZYC
ALIPV
ALMA_UNASSIGNED_HOLDINGS
AOIJS
AZQEC
BAWUL
BBNVY
BCNDV
BENPR
BHPHI
BPHCQ
BVXVI
CCPQU
CS3
D1I
DIK
DU5
DWQXO
E3Z
EBD
EBS
EJD
ESTFP
ESX
F5P
FRP
FYUFA
GNUQQ
GROUPED_DOAJ
GUQSH
GX1
HCIFZ
HH5
HMCUK
HYE
IAO
ITC
KB.
KQ8
LK8
M1P
M2O
M48
M7P
MODMG
M~E
NPM
O5R
O5S
OK1
P2P
PDBOC
PIMPY
PQQKQ
PROAC
PSQYO
RIG
RNS
RPM
TR2
TUS
UKHRP
~8M
AAYXX
AFPKN
CITATION
7XB
8FK
K9.
MBDVC
PQEST
PQUKI
PRINS
Q9U
7X8
5PM
ID FETCH-LOGICAL-c3933-1ae97970db153d8da6901130690c2368e523dca49b106077ef04b0927d320cd3
IEDL.DBID RPM
ISSN 1422-0067
1661-6596
IngestDate Tue Oct 22 15:12:12 EDT 2024
Tue Sep 17 21:02:43 EDT 2024
Sat Oct 05 05:13:24 EDT 2024
Tue Oct 15 13:42:15 EDT 2024
Wed Jul 31 12:43:08 EDT 2024
Wed Oct 16 00:41:06 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 11
Keywords secondary structure
time-resolved fluorescence
FTIR technique
gliadin
phenolic acids
Language English
License Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c3933-1ae97970db153d8da6901130690c2368e523dca49b106077ef04b0927d320cd3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ORCID 0000-0003-0784-898X
0000-0001-8618-2092
0000-0001-7712-0041
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9181179/
PMID 35682729
PQID 2674360493
PQPubID 2032341
ParticipantIDs doaj_primary_oai_doaj_org_article_bb165a168cab41b0ae8a6cec555dad6f
pubmedcentral_primary_oai_pubmedcentral_nih_gov_9181179
proquest_miscellaneous_2675610301
proquest_journals_2674360493
crossref_primary_10_3390_ijms23116053
pubmed_primary_35682729
PublicationCentury 2000
PublicationDate 20220527
PublicationDateYYYYMMDD 2022-05-27
PublicationDate_xml – month: 5
  year: 2022
  text: 20220527
  day: 27
PublicationDecade 2020
PublicationPlace Switzerland
PublicationPlace_xml – name: Switzerland
– name: Basel
PublicationTitle International journal of molecular sciences
PublicationTitleAlternate Int J Mol Sci
PublicationYear 2022
Publisher MDPI AG
MDPI
Publisher_xml – name: MDPI AG
– name: MDPI
References Khan (ref_5) 2017; 7
Mazzaracchio (ref_10) 2011; 129
Sivam (ref_9) 2012; 131
ref_14
Mulaudzi (ref_13) 2012; 143
Nawrocka (ref_7) 2016; 64
Nawrocka (ref_8) 2017; 231
Tozzi (ref_12) 2013; 141
Cao (ref_21) 2012; 51
Taddei (ref_11) 2013; 44
Albani (ref_24) 2014; 24
Adamcik (ref_19) 2018; 57
Wang (ref_26) 2020; 229
Nawrocka (ref_15) 2018; 252
Juszczyk (ref_17) 2009; 15
Fraga (ref_3) 2019; 10
Wrigley (ref_1) 1973; 209
ref_23
Kanakis (ref_28) 2011; 127
Sato (ref_22) 2013; 288
Skrt (ref_27) 2012; 135
Velander (ref_20) 2017; 139
Stevenson (ref_25) 1994; 71
Elzoghby (ref_2) 2012; 161
Glei (ref_6) 2006; 56
Yan (ref_4) 2020; 6
Secundo (ref_16) 2005; 53
Cao (ref_18) 2019; 269
References_xml – ident: ref_14
  doi: 10.3390/molecules26020508
– volume: 10
  start-page: 514
  year: 2019
  ident: ref_3
  article-title: The Effects of Polyphenols and Other Bioactives on Human Health
  publication-title: Food Funct.
  doi: 10.1039/C8FO01997E
  contributor:
    fullname: Fraga
– volume: 139
  start-page: 40
  year: 2017
  ident: ref_20
  article-title: Natural Product-Based Amyloid Inhibitors
  publication-title: Biochem. Pharmacol.
  doi: 10.1016/j.bcp.2017.04.004
  contributor:
    fullname: Velander
– volume: 141
  start-page: 3586
  year: 2013
  ident: ref_12
  article-title: Study on the Interaction between Gliadins and a Coumarin as Molecular Model System of the Gliadins–Anthocyanidins Complexes
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2013.05.136
  contributor:
    fullname: Tozzi
– volume: 71
  start-page: 155
  year: 1994
  ident: ref_25
  article-title: Intrinsic Fluorescence and Quenching Studies of Gluten Proteins
  publication-title: Cereal Chem.
  contributor:
    fullname: Stevenson
– volume: 231
  start-page: 51
  year: 2017
  ident: ref_8
  article-title: Aggregation of Gluten Proteins in Model Dough after Fibre Polysaccharide Addition
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2017.03.117
  contributor:
    fullname: Nawrocka
– volume: 7
  start-page: 9470
  year: 2017
  ident: ref_5
  article-title: Elucidation of Dietary Polyphenolics as Potential Inhibitor of Microtubule Affinity Regulating Kinase 4: In Silico and In Vitro Studies
  publication-title: Sci. Rep.
  doi: 10.1038/s41598-017-09941-4
  contributor:
    fullname: Khan
– volume: 288
  start-page: 23212
  year: 2013
  ident: ref_22
  article-title: Site-Specific Inhibitory Mechanism for Amyloid Β42 Aggregation by Catechol-Type Flavonoids Targeting the Lys Residues *
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M113.464222
  contributor:
    fullname: Sato
– ident: ref_23
  doi: 10.1007/978-1-4757-3061-6
– volume: 56
  start-page: 182
  year: 2006
  ident: ref_6
  article-title: Bread Enriched with Green Coffee Extract Has Chemoprotective and Antigenotoxic Activities in Human Cells
  publication-title: Nutr. Cancer
  doi: 10.1207/s15327914nc5602_9
  contributor:
    fullname: Glei
– volume: 57
  start-page: 8370
  year: 2018
  ident: ref_19
  article-title: Amyloid Polymorphism in the Protein Folding and Aggregation Energy Landscape
  publication-title: Angew. Chem. Int. Ed.
  doi: 10.1002/anie.201713416
  contributor:
    fullname: Adamcik
– volume: 44
  start-page: 1435
  year: 2013
  ident: ref_11
  article-title: Raman Characterization of the Interactions between Gliadins and Anthocyanins
  publication-title: J. Raman Spectrosc.
  doi: 10.1002/jrs.4288
  contributor:
    fullname: Taddei
– volume: 15
  start-page: 23
  year: 2009
  ident: ref_17
  article-title: FTIR Spectroscopic Studies on Aggregation Process of the Beta-Amyloid 11-28 Fragment and Its Variants
  publication-title: J. Pept. Sci.
  doi: 10.1002/psc.1085
  contributor:
    fullname: Juszczyk
– volume: 135
  start-page: 2418
  year: 2012
  ident: ref_27
  article-title: Interactions of Different Polyphenols with Bovine Serum Albumin Using Fluorescence Quenching and Molecular Docking
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2012.06.114
  contributor:
    fullname: Skrt
– volume: 131
  start-page: 802
  year: 2012
  ident: ref_9
  article-title: Exploring the Interactions between Blackcurrant Polyphenols, Pectin and Wheat Biopolymers in Model Breads; a FTIR and HPLC Investigation
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2011.09.047
  contributor:
    fullname: Sivam
– volume: 161
  start-page: 38
  year: 2012
  ident: ref_2
  article-title: Protein-Based Nanocarriers as Promising Drug and Gene Delivery Systems
  publication-title: J. Control. Release
  doi: 10.1016/j.jconrel.2012.04.036
  contributor:
    fullname: Elzoghby
– volume: 129
  start-page: 1100
  year: 2011
  ident: ref_10
  article-title: Interaction between Gliadins and Anthocyan Derivatives
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2011.05.084
  contributor:
    fullname: Mazzaracchio
– volume: 127
  start-page: 1046
  year: 2011
  ident: ref_28
  article-title: Milk β-Lactoglobulin Complexes with Tea Polyphenols
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2011.01.079
  contributor:
    fullname: Kanakis
– volume: 24
  start-page: 93
  year: 2014
  ident: ref_24
  article-title: Origin of Tryptophan Fluorescence Lifetimes Part 1. Fluorescence Lifetimes Origin of Tryptophan Free in Solution
  publication-title: J. Fluoresc.
  doi: 10.1007/s10895-013-1277-8
  contributor:
    fullname: Albani
– volume: 53
  start-page: 1757
  year: 2005
  ident: ref_16
  article-title: ATR-FT/IR Study on the Interactions between Gliadins and Dextrin and Their Effects on Protein Secondary Structure
  publication-title: J. Agric. Food Chem.
  doi: 10.1021/jf049061x
  contributor:
    fullname: Secundo
– volume: 64
  start-page: 2094
  year: 2016
  ident: ref_7
  article-title: Dietary Fiber-Induced Changes in the Structure and Thermal Properties of Gluten Proteins Studied by Fourier Transform-Raman Spectroscopy and Thermogravimetry
  publication-title: J. Agric. Food Chem.
  doi: 10.1021/acs.jafc.5b05712
  contributor:
    fullname: Nawrocka
– volume: 143
  start-page: 185
  year: 2012
  ident: ref_13
  article-title: Pharmacological Properties and Protein Binding Capacity of Phenolic Extracts of Some Venda Medicinal Plants Used against Cough and Fever
  publication-title: J. Ethnopharmacol.
  doi: 10.1016/j.jep.2012.06.022
  contributor:
    fullname: Mulaudzi
– volume: 229
  start-page: 117937
  year: 2020
  ident: ref_26
  article-title: Interaction between Wheat Gliadin and Quercetin under Different PH Conditions Analyzed by Multi-Spectroscopy Methods
  publication-title: Spectrochim. Acta A Mol. Biomol. Spectrosc.
  doi: 10.1016/j.saa.2019.117937
  contributor:
    fullname: Wang
– volume: 51
  start-page: 2670
  year: 2012
  ident: ref_21
  article-title: Analysis of the Inhibition and Remodeling of Islet Amyloid Polypeptide Amyloid Fibers by Flavanols
  publication-title: Biochemistry
  doi: 10.1021/bi2015162
  contributor:
    fullname: Cao
– volume: 269
  start-page: 334
  year: 2019
  ident: ref_18
  article-title: Food Protein Amyloid Fibrils: Origin, Structure, Formation, Characterization, Applications and Health Implications
  publication-title: Adv. Colloid Interface Sci.
  doi: 10.1016/j.cis.2019.05.002
  contributor:
    fullname: Cao
– volume: 6
  start-page: 115
  year: 2020
  ident: ref_4
  article-title: Antioxidant Mechanism of Tea Polyphenols and Its Impact on Health Benefits
  publication-title: Anim. Nutr.
  doi: 10.1016/j.aninu.2020.01.001
  contributor:
    fullname: Yan
– volume: 209
  start-page: 154
  year: 1973
  ident: ref_1
  article-title: Electrofocusing of Grain Proteins from Wheat Genotypes
  publication-title: Ann. N. Y. Acad. Sci.
  doi: 10.1111/j.1749-6632.1973.tb47526.x
  contributor:
    fullname: Wrigley
– volume: 252
  start-page: 198
  year: 2018
  ident: ref_15
  article-title: FTIR Studies of Gluten Matrix Dehydration after Fibre Polysaccharide Addition
  publication-title: Food Chem.
  doi: 10.1016/j.foodchem.2018.01.110
  contributor:
    fullname: Nawrocka
SSID ssj0023259
Score 2.402822
Snippet The effect of the chemical structure of selected phenolic acids on the molecular organization of gliadins was investigated with the application of Fourier...
SourceID doaj
pubmedcentral
proquest
crossref
pubmed
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
StartPage 6053
SubjectTerms Amino acids
Chains
Disaggregation
Fluorescence spectroscopy
Fourier transforms
FTIR technique
Gliadin
Gluten
Hydrocarbons
Hydrogen bonds
Hydrophobicity
Hydroxycinnamic acid
Lifetime
Molecular weight
Phenolic acids
Polypeptides
Polyphenols
Protein structure
Proteins
secondary structure
Spectrum analysis
Stiffness
Tertiary structure
time-resolved fluorescence
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Na9tAEF1KINBLyUeTqEnKFpqj8GpXu9KegpM0MYWWgh3ITeyXiEMqGdsh5Afkf2dGkl07FHLJydhapLVmduc9aeYNId-1dMZqq2ClAUVJMWlHe6FjzZlXNoMYp7DA-ddvNbhOf97Im5VWX5gT1soDtzeuZ22ipElUDudME8tMyI1ywUkpvfGqbHZfphdkqqNagjdt0hKIPrGSWrUp7wIIfm9893cGoCYBHC_WglGj2f8_oPk6X3IlAF1ukU8dcqT9dsbb5EOodshm20vyaZc8D-pHelHTP7ehQq1f2ndjP6Nt9QAFmEeHyH29mT5RU3k6woRq_DJsFGQfpoHWJb26H2NS_Snt8gspPqeF8bT_70U3jsO29XMUwqwncKnRQgh29pmMLn-Mzgdx12MhdkILEScm6ExnzFvY-nzuDTaogrgGH44LlQcgqt6ZVFvgjizLQslSyzTPvODMebFHNqq6CgeElszKNHBpbSnSMuNwJmkcB7xoS8CZLiIni3tdTFoljQIYCNqkWLVJRM7QEMsxqH_d_ABeUXReUbzlFRE5Wpix6BblrOBYcKGAEsE1vi0Pw3LCdySmCvVDMwYRJWx7Edlvrb6ciZAq50BGIpKt-cPaVNePVOPbRrJbJ1jQq7-8x387JB851mAwLCY8IhvgJeEYkNHcfm0WwQvV3w3q
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: ProQuest Central
  dbid: BENPR
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwEB7BVkhcEG8CBRkJjlEdO3biU7WFlhUSVUUXqbfIr9BFkCybVqg_gP_NTJLddhHiFCW2Eisz9nyfPQ-AN0Z564zTONOQouTktGOCNKkRPGhXoI3TFOD86VjPvuQfz9TZuOHWjW6V6zWxX6hD62mPfE-Qt7xGPCv3lz9TqhpFp6tjCY3bsCOQKfAJ7BwcHp983lAuKfpyaRlaoVQrowfXd4lEf2_x7UeH4CZDPC-3jFKfu_9fgPNvv8kbhujoPtwbESSbDiJ_ALdi8xDuDDUlrx7B71n7i71v2cl5bCjnL5v6RejYEEXAEO6xU-LAwa6umG0Cm5NjNd2c9plkL1eRtTX78H1BzvX7bPQzZLRfi_3Z9PrAm_pR-foLSojZLvFT83VC2O4xzI8O5-9m6VhrIfXSSJlmNprCFDw4XAJDGSwVqkL7hhcvpC4jEtbgbW4cckheFLHmueNGFEEK7oN8ApOmbeIzYDV3Ko9COVfLvC4EvklZLxA3uhrxpk_g7fpfV8sho0aFTIRkUt2USQIHJIhNH8qD3T9oV1-rcVpVzmVa2UyXqHF55riNpdU-eqVUsEHXCeyuxViNk7OrrlUpgdebZpxWdFZim9he9n0IWeLyl8DTQeqbkUilS4GkJIFiSx-2hrrd0izO-9TdJqPAXvP8_8N6AXcFRVlwChfchQnKP75E7HPhXo0K_geLVQTw
  priority: 102
  providerName: ProQuest
– databaseName: Scholars Portal Journals: Open Access
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV1Jb9QwFH4qRUhcKnYCBRkJjoHEW-IDqoaljJBASJ1KvUXeQgeVpJ1pBfMD-N-8l2XoQA-coiRObPk9299nvwXguVHeOuM0jjSkKJKMdkwQJjU8C9oVuMZpcnD-9FlPD-XHI3W0BWO20aEDl1dSO8ondbg4efnzbLWHA_41MU6k7K_m374vEabkiMzFNbjOJXJ0MuKT6_MEhA1d2jTa8Ehpgu5N4P_5emNx6mL4XwU8_7afvLQg7d-CnQFJskkv-tuwFZs7cKPPLbm6C7-m7Q_2rmVfjmNDsX_ZxM_DkvXeBAxhHzsgLhzsYsVsE9iMDKzp5qCLKHuxiKyt2YeTORnZ77HB3pDRvi2WZ5M_B99UjtLYn1NgzPYUq5qNgWGX92C2_372dpoOORdSL4wQaW6jKUyRBYdTYSiDpYRVuM7hxXOhy4jENXgrjUMumRVFrDPpMsOLIHjmg7gP203bxIfA6swpGblyrhayLjj-SVnPET-6GnGnT-DF2NfVaR9Zo0JGQjKpLsskgTckiHUZiofdPWgXX6theFXO5VrZXJeoeTJ3mY2l1T56pVSwQdcJ7I5irEYdqzg5YGikSFjHs_VrHF50ZmKb2F50ZQhh4jSYwINe6uuWCKVLjuQkgWJDHzaauvmmmR93IbxNTg6-5tF_9sFjuMnJ7SIj_8Fd2EZFiE8QDJ27p52e_wb6MQjS
  priority: 102
  providerName: Scholars Portal
Title How Do Phenolic Acids Change the Secondary and Tertiary Structure of Gliadin? Studies with an Application of Spectroscopic Techniques
URI https://www.ncbi.nlm.nih.gov/pubmed/35682729
https://www.proquest.com/docview/2674360493
https://search.proquest.com/docview/2675610301
https://pubmed.ncbi.nlm.nih.gov/PMC9181179
https://doaj.org/article/bb165a168cab41b0ae8a6cec555dad6f
Volume 23
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9NAEF61RUhcEG8MxVokOKaxd71r7wmlpWmElCqiQcrN2pdbo8aOklaoP4D_zYwfaYM4cbGVeBOvPLOe77O_mSHkkxJWG2UkrDSgKAmKdpTjaqBY5KRJIcZJTHCensvJj-TbQiz2iOhzYRrRvjXlUXW9PKrKq0ZbuVraYa8TG86mJyrG9Eg13Cf74KA9Re9YFgdA3yrcOfD5YflzuQEMEwNsx545XMiMtYDyPgw11fr_BTH_Vko-CD3jZ-RphxnpqJ3bc7LnqxfkcdtF8u4l-T2pf9GvNZ1d-Qqr_NKRLd2GtnkDFAAevUDW6_T6jurK0TlKqfHDRVM79nbtaV3Qs-sS5fRfaKcspPiEFsbT0f0rbhyHDetvsARmvYJTzfsSsJtXZD4-nZ9MBl13hYHlivNBrL1KVRo5Azc9lzmNrakgosHOMi4zDxTVWZ0oA6wxSlNfRImJFEsdZ5F1_DU5qOrKvyW0iIxIPBPGFDwpUgb_JLRlgBRNAQjTBuRzf63zVVtDIwfugebJH5onIMdoiO0YrHzdfFGvL_PO_rkxsRQ6lhn4WBKbSPtMS-utEMJpJ4uAHPZmzLvluMkZplpIIENwjo_bw7CQ8O2Irnx924xBLAk3vIC8aa2-nUnvNQFJd_xhZ6q7R8B3m2Ldna----9fvidPGKZcRJg7eEgOwDX8BwBCNyYE91-ksM3GZyF5dHx6PvseNg8VQgxQArbTJAub5fEHvEAQzw
link.rule.ids 230,315,730,783,787,867,888,2109,2228,12068,12777,21400,24330,27936,27937,31731,31732,33385,33386,33756,33757,43322,43612,43817,53804,53806,74079,74369,74636
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwEB5BEYIL4k2ggJHgGDWxYyc-VcujLNBWSA3S3iK_QhdBsmxaof4A_jczSXa3ixCnKLGVWJmx5xt75huAl1o6Y7VVONPQRckoaEd7oWPNE69sjjZOUYLz0bGafsk-zuRs3HDrxrDK1ZrYL9S-dbRHvscpWl4hnhX7i58xVY2i09WxhMZVuEY8XFTBIJ9tHC7B-2JpKdqgWEmthsB3gW7-3vzbjw6hTYpoXmyZpJ65_19w8--oyUtm6OA23BrxI5sMAr8DV0JzF64PFSUv7sHvafuLvW3Z59PQEOMvm7i579iQQ8AQ7LET8oC9WV4w03hWUlg13Zz0PLLny8Damr3_PqfQ-n02Rhky2q3F_myyOe6mflS8_ozoMNsFfqpc0cF296E8eFe-mcZjpYXYCS1EnJqgc50n3uIC6AtvqEwVWje8OC5UEdBd9c5k2qIHmeR5qJPMJprnXvDEefEAdpq2CY-A1YmVWeDS2lpkdc7xTdI4jqjR1og2XQSvVv-6Wgx8GhX6ISST6rJMInhNglj3IRbs_kG7_FqNk6qyNlXSpKpAfctSm5hQGOWCk1J641Udwe5KjNU4Nbtqo0gRvFg346SikxLThPa870O4Ehe_CB4OUl-PREhVcHRJIsi39GFrqNstzfy0J-7WKaX16sf_H9ZzuDEtjw6rww_Hn57ATU75FgklDu7CDupCeIoo6Mw-61X9D5ccBns
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Lb9QwEB5BEYgL4lkCBYwEx2gTO3biU7VQtsurqtRF6i3yK3RRmyybVqg_gP_NTJLddhHiFCUZJVZm7Pkm_mYG4I2WzlhtFc40DFEyIu1oL3SseeKVzdHHKUpw_nqgpt-yT8fyeOA_tQOtcrUmdgu1bxz9Ix9xYssrxLNiVA20iMO9ye7iZ0wdpGindWincRNukSRZeDHZXwdfgneN01L0R7GSWvUkeIEh_2j-46xFmJMishcb7qmr4v8v6Pk3g_KaS5rch3sDlmTjXvkP4EaoH8Ltvrvk5SP4PW1-sb2GHZ6Emqr_srGb-5b1-QQMgR87omjYm-UlM7VnM6JY08lRV1P2YhlYU7H90znR7HfZwDhk9OcW5dn4auub5KiR_TmVxmwW-KrZqjRs-xhmkw-z99N46LoQO6GFiFMTdK7zxFtcDH3hDbWsQk-HB8eFKgKGrt6ZTFuMJpM8D1WS2UTz3AueOC-ewFbd1OEpsCqxMgtcWluJrMo5PkkaxxFB2gqRp4vg7epbl4u-tkaJMQnppLyukwjekSLWMlQRu7vQLL-XwwQrrU2VNKkq0Pay1CYmFEa54KSU3nhVRbCzUmM5TNO2vDKqCF6vb-MEo10TU4fmopMhjIkLYQTbvdbXIxFSFRzDkwjyDXvYGOrmnXp-0hXx1iml-Opn_x_WK7iDVl5--Xjw-Tnc5ZR6kVAO4Q5soSmEFwiIzu3LztL_AO8uCrk
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=How+Do+Phenolic+Acids+Change+the+Secondary+and+Tertiary+Structure+of+Gliadin%3F+Studies+with+an+Application+of+Spectroscopic+Techniques&rft.jtitle=International+journal+of+molecular+sciences&rft.au=Welc%2C+Renata&rft.au=Luchowski%2C+Rafa%C5%82&rft.au=K%C5%82osok%2C+Konrad&rft.au=Gruszecki%2C+Wies%C5%82aw+I.&rft.date=2022-05-27&rft.issn=1422-0067&rft.eissn=1422-0067&rft.volume=23&rft.issue=11&rft.spage=6053&rft_id=info:doi/10.3390%2Fijms23116053&rft.externalDBID=n%2Fa&rft.externalDocID=10_3390_ijms23116053
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1422-0067&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1422-0067&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1422-0067&client=summon