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Published on: July 27, 2016
Protein-tannins binding mode in hydrolyzable tannins-induced protein aggregation
Mana Yoshimura1, Yoshiki Sugahara1, Kana Nagase1
1Faculty of Applied Biological Sciences, Gifu University, Gifu, Gifu 501-1193, Japan.
None:
Because the interaction between proteins and tannins is complex, the mode of binding has not yet been elucidated. Elucidating this interaction has been considered impossible to accomplish, especially in water, in which proteins retain their three-dimensional (3D) structure. In this study, a combination of molecular dynamics (MD) simulations of multiple molecules and 1H15N heteronuclear single quantum coherence (HSQC) NMR was used to elucidate the mode of interaction. The simulations revealed that tannins are bound via water molecules rather than directly to proteins. In addition, the simulations showed that the locations with many hydrogen bonds between proteins and tannins coincided with the locations where the HSQC chemical shift changes occurred. These results revealed the protein-binding positions of tannins, suggesting that protein-protein binding and aggregation occur through these bonds. These results advance the understanding of the astringency and bioactivity of polyphenols at a molecular level.
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