DYNAMIC AND TOPOLOGY OF PROTEIN/POLYPHENOL MOLECULAR INTERACTIONS

ANDRE NICOLAI PETELSKI; SILVANA CARINA PAMIES; GLADIS LAURA SOSA

Santiago

Congreso; 10th Triennial Congress of the World Association of Theoretical and Computational Chemists; 2014

World Association of Theoretical and Computational Chemists

Molecular interactions between polyphenols and proteins lead to three well known phenomena. In beverages like beer the interactions between proline rich proteins and polyphenols, cause colloidal turbidity. On the other hand, when natural polyphenols of some beverages, like wine or tea, enter the oral cavity they interact with salivary proteins (rich in proline) to produce a mouth feeling called astringency. Also, it has been observed that flavonoids can inhibit enzymes when they reach the tract digestive. Finally, in leather industry, these interactions are well exploited by using natural tannins that bind to collagen skin to produce leather. However, the understanding of these interactions is still target of many researches. For the purpose to contribute to the comprehension of these interactions, in this work we studied a protein/polyphenol complex solvated in water with different theoretical tools. The selected complex was formed by a protein fragment of a collagen chain (A189) and the flavonoid procianidin C1 (PC1); the system was then solvated with molecules of water. The mechanism of formation of colloidal particles has been examined with molecular dynamic simulations using the AMBER 11 package. Then, a structure of the MD was obtained to perform a deep analysis of the interactions involved in the complex by the Quantum Theory of Atoms In Molecules (QTAIM) of Bader. The wave function was obtained at the B3LYP/631G* level of theory.