The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols.

Antigens, Plant / chemistry Circular Dichroism Food Quality Models, Molecular Polyphenols / chemistry Protein Binding Protein Structure, Secondary Thermodynamics Transition Temperature Vitis / chemistry
Synchrotron Radiation Circular Dichroism (SRCD) VVTL1 polyphenols protein interaction protein structure wine

Journal

Molecules (Basel, Switzerland)
ISSN: 1420-3049
Titre abrégé: Molecules
Pays: Switzerland
ID NLM: 100964009

Informations de publication

Date de publication:
03 Apr 2020
Historique:
received: 20 03 2020
revised: 01 04 2020
accepted: 01 04 2020
entrez: 9 4 2020
pubmed: 9 4 2020
medline: 20 1 2021
Statut: epublish

Résumé

Polyphenols are an important constituent of wines and they are largely studied due to their antioxidant properties and for their effects on wine quality and stability, which is also related to their capacity to bind to proteins. The effects of some selected polyphenols, including procyanidins B1 and B2, tannic acid, quercetin, and rutin, as well as those of a total white wine procyanidin extract on the conformational properties of the major wine protein VVTL1 (

Identifiants

DOI: 10.3390/molecules25071646 PMID: 32260104 PMC: PMC7180857
pubmed: 32260104
pii: molecules25071646
doi: 10.3390/molecules25071646
pmc: PMC7180857
pii:
doi:

Substances chimiques

Antigens, Plant 0
Polyphenols 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Références

J Food Sci Technol. 2020 Jul;57(7):2602-2611
pubmed: 32549610
J Agric Food Chem. 2007 Feb 7;55(3):992-1002
pubmed: 17263504
Am J Clin Nutr. 2005 Jan;81(1 Suppl):223S-229S
pubmed: 15640485
J Agric Food Chem. 2009 May 27;57(10):4328-33
pubmed: 19385597
J Agric Food Chem. 1999 Feb;47(2):353-62
pubmed: 10563900
Biochim Biophys Acta. 2016 Oct;1860(10):2239-48
pubmed: 27133445
J Agric Food Chem. 2011 Mar 23;59(6):2652-62
pubmed: 21361294
J Agric Food Chem. 2010 Jan 27;58(2):975-80
pubmed: 20014848
Molecules. 2019 Jun 11;24(11):
pubmed: 31212597
J Agric Food Chem. 2011 Jan 26;59(2):733-40
pubmed: 21189017
J Agric Food Chem. 2011 Jul 13;59(13):6871-6
pubmed: 21627320
J Comput Chem. 2004 Oct;25(13):1605-12
pubmed: 15264254
J Agric Food Chem. 2012 Oct 24;60(42):10666-73
pubmed: 22998638
Magn Reson Chem. 2006 Sep;44(9):868-80
pubmed: 16791908
Food Chem. 2012 Jul 15;133(2):423-9
pubmed: 25683415
Crit Rev Food Sci Nutr. 2012;52(3):213-48
pubmed: 22214442
J Agric Food Chem. 2009 Dec 9;57(23):11376-82
pubmed: 19886666
ACS Omega. 2020 Feb 17;5(8):4293-4301
pubmed: 32149259
J Agric Food Chem. 2016 Feb 17;64(6):1309-17
pubmed: 26806526
Amino Acids. 2010 Jun;39(1):285-96
pubmed: 20091070
Biochemistry. 1981 Jan 6;20(1):33-7
pubmed: 7470476
FASEB J. 2010 Nov;24(11):4281-90
pubmed: 20605948
J Agric Food Chem. 2015 Apr 29;63(16):4020-30
pubmed: 25847216
J Synchrotron Radiat. 2015 Mar;22(2):465-8
pubmed: 25723950
PLoS One. 2012;7(7):e40548
pubmed: 22802966
Adv Protein Chem Struct Biol. 2019;118:413-436
pubmed: 31928733
Biophys Rev. 2017 Oct;9(5):517-527
pubmed: 28825203
Methods Mol Biol. 2005;305:343-64
pubmed: 15940006
J Agric Food Chem. 2010 Dec 8;58(23):12510-8
pubmed: 21070019
Crit Rev Food Sci Nutr. 2019;59(13):2072-2094
pubmed: 29420057
Chem Rev. 2007 Aug;107(8):3514-43
pubmed: 17683160
Molecules. 2018 Jul 31;23(8):
pubmed: 30065161
Biomolecules. 2015 May 04;5(2):724-34
pubmed: 25946077
Anal Chim Acta. 2010 Feb 15;660(1-2):110-8
pubmed: 20103151
Food Chem. 2017 Feb 15;217:373-378
pubmed: 27664648
Eur J Biochem. 1994 Feb 1;219(3):923-35
pubmed: 8112344
J Agric Food Chem. 2014 Jul 30;62(30):7515-23
pubmed: 25017417
PLoS One. 2014 Dec 02;9(12):e113757
pubmed: 25463627
Biochim Biophys Acta. 2006 Jun;1760(6):951-8
pubmed: 16527409

Auteurs

Mattia Di Gaspero (M)

Department of Land, Environment, Agriculture and Forestry (TESAF), University of Padua, Viale dell'Università, 16, 35020 Legnaro (PD), Italy.

Paolo Ruzza (P)

Institute of Biomolecular Chemistry of CNR, Padua Unit, via Marzolo 1, 35131 Padua, Italy.
ORCID: 0000-0002-5596-9295

Rohanah Hussain (R)

Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK.

Claudia Honisch (C)

Institute of Biomolecular Chemistry of CNR, Padua Unit, via Marzolo 1, 35131 Padua, Italy.
Department of Chemical Sciences, University of Padua, Via Marzolo 1, 35131 Padua, Italy.

Barbara Biondi (B)

Institute of Biomolecular Chemistry of CNR, Padua Unit, via Marzolo 1, 35131 Padua, Italy.
ORCID: 0000-0003-2393-7333

Giuliano Siligardi (G)

Diamond Light Source Ltd., Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, UK.
ORCID: 0000-0002-4667-6423

Matteo Marangon (M)

Department of Agronomy, Food, Natural Resources Animals and Environment (DAFNAE), University of Padua, Viale dell'Università, 16, 35020 Legnaro (PD), Italy.
ORCID: 0000-0001-5358-2428

Andrea Curioni (A)

Department of Agronomy, Food, Natural Resources Animals and Environment (DAFNAE), University of Padua, Viale dell'Università, 16, 35020 Legnaro (PD), Italy.

Simone Vincenzi (S)

Department of Agronomy, Food, Natural Resources Animals and Environment (DAFNAE), University of Padua, Viale dell'Università, 16, 35020 Legnaro (PD), Italy.

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Classifications MeSH

questionsmedicales.fr › Facteurs biologiques › Antigènes › Antigènes végétaux › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Analyse spectrale › Dichroïsme circulaire › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Environnement et santé publique › Santé publique › Qualité alimentaire › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Composés chimiques organiques › Hydrocarbures › Hydrocarbures cycliques › Hydrocarbures aromatiques › Dérivés du benzène › Phénols › Polyphénols › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Métabolisme › Liaison aux protéines › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure secondaire des protéines › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Phénomènes physiques › Thermodynamique › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Phénomènes physiques › Thermodynamique › Température de transition › The Secondary Structure of a Major Wine...
questionsmedicales.fr › Eucaryotes › Viridiplantae › Streptophyta › Embryophyta › Tracheobionta › Magnoliopsida › Vitaceae › Vitis › The Secondary Structure of a Major Wine...