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

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...

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Autores principales: Di Gaspero, Mattia, Ruzza, Paolo, Hussain, Rohanah, Honisch, Claudia, Biondi, Barbara, Siligardi, Giuliano, Marangon, Matteo, Curioni, Andrea, Vincenzi, Simone
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7180857/
https://www.ncbi.nlm.nih.gov/pubmed/32260104
http://dx.doi.org/10.3390/molecules25071646
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author Di Gaspero, Mattia
Ruzza, Paolo
Hussain, Rohanah
Honisch, Claudia
Biondi, Barbara
Siligardi, Giuliano
Marangon, Matteo
Curioni, Andrea
Vincenzi, Simone
author_facet Di Gaspero, Mattia
Ruzza, Paolo
Hussain, Rohanah
Honisch, Claudia
Biondi, Barbara
Siligardi, Giuliano
Marangon, Matteo
Curioni, Andrea
Vincenzi, Simone
author_sort Di Gaspero, Mattia
collection PubMed
description 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 (Vitis vinifera Thaumatin-Like-1) were investigated by Synchrotron Radiation Circular Dichroism (SRCD). Results showed that VVTL1 interacts with polyphenols as demonstrated by the changes in the secondary (far-UV) and tertiary (near-UV) structures, which were differently affected by different polyphenols. Additionally, polyphenols modified the two melting temperatures (T(M)) that were found for VVTL1 (32.2 °C and 53.9 °C for the protein alone). The circular dichroism (CD) spectra in the near-UV region revealed an involvement of the aromatic side-chains of the protein in the interaction with phenolics. The data demonstrate the existence of an interaction between polyphenols and VVTL1, which results in modification of its thermal and UV denaturation pattern. This information can be useful in understanding the behavior of wine proteins in presence of polyphenols, thus giving new insights on the phenomena that are involved in wine stability.
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spelling pubmed-71808572020-05-01 The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols Di Gaspero, Mattia Ruzza, Paolo Hussain, Rohanah Honisch, Claudia Biondi, Barbara Siligardi, Giuliano Marangon, Matteo Curioni, Andrea Vincenzi, Simone Molecules Article 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 (Vitis vinifera Thaumatin-Like-1) were investigated by Synchrotron Radiation Circular Dichroism (SRCD). Results showed that VVTL1 interacts with polyphenols as demonstrated by the changes in the secondary (far-UV) and tertiary (near-UV) structures, which were differently affected by different polyphenols. Additionally, polyphenols modified the two melting temperatures (T(M)) that were found for VVTL1 (32.2 °C and 53.9 °C for the protein alone). The circular dichroism (CD) spectra in the near-UV region revealed an involvement of the aromatic side-chains of the protein in the interaction with phenolics. The data demonstrate the existence of an interaction between polyphenols and VVTL1, which results in modification of its thermal and UV denaturation pattern. This information can be useful in understanding the behavior of wine proteins in presence of polyphenols, thus giving new insights on the phenomena that are involved in wine stability. MDPI 2020-04-03 /pmc/articles/PMC7180857/ /pubmed/32260104 http://dx.doi.org/10.3390/molecules25071646 Text en © 2020 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 (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Di Gaspero, Mattia
Ruzza, Paolo
Hussain, Rohanah
Honisch, Claudia
Biondi, Barbara
Siligardi, Giuliano
Marangon, Matteo
Curioni, Andrea
Vincenzi, Simone
The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols
title The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols
title_full The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols
title_fullStr The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols
title_full_unstemmed The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols
title_short The Secondary Structure of a Major Wine Protein is Modified upon Interaction with Polyphenols
title_sort secondary structure of a major wine protein is modified upon interaction with polyphenols
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7180857/
https://www.ncbi.nlm.nih.gov/pubmed/32260104
http://dx.doi.org/10.3390/molecules25071646
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