Recognition characters in peptide–polyphenol complex formation |
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| Authors: | T. Richard D. Lefeuvre A. Descendit S. Quideau J.P. Monti |
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| Affiliation: | 1. Laboratoire de physique et biophysique, Université de Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux cedex, France;2. Laboratoire de biotechnologie végétale GESVAB EA 3675, Université de Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux cedex, France;3. Centre de Recherche en Chimie Moléculaire, Laboratoire de Chimie Organique et Organométallique (CNRS UMR 5802), Université Bordeaux 1, 351 cours de la Libération, 33405 Talence cedex, France et Institut Européen de Chimie et Biologie, 2 rue Robert Escarpit, 33607 Pessac cedex, France |
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| Abstract: | Dietary polyphenols have received attention for their anti-oxidative, anti-carcinogenic and anti-neurodegenerative effects. Polyphenols bind to proteins leading to the formation of soluble or insoluble protein–polyphenol complexes which could significantly influence their biological activities. NMR and molecular modeling studies were performed to investigate the influence of the bulk, flexibility and hydrophobicity of polyphenols on the association with bradykinin, the peptide model. Our results show that the strength of the interactions could be positively correlated with polyphenol hydrophobicity and a comparison between pentagalloylglucose and vescalagin indicated that flexibility might play a positive role in the interaction with peptides and proteins. |
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| Keywords: | Bradykinin Polyphenol NMR |
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