How procyanidin C1 sticks to collagen: The role of proline rings

Molecular interactions between proteins and polyphenols are responsible for many natural phenomena like colloidal turbidity, astringency, denaturation of enzymes and leather tanning. Although these phenomena are well known, there are open questions about the specific interactions involved in the complexation process. In this work, Molecular Dynamic (MD) simulations and the topology of the electron density analysis were used to study the interactions between the flavonoid procyanidin C1 and a collagen fragment solvated in water. Root mean square deviation; root mean square fluctuation and hydrogen bonds occupancy were examined after 50 ns. The interactions were also analyzed by means of the quantum theory of atoms in molecules. Our results show that the main interactions are hydrogen bonds between -OH groups of the polyphenol and CO groups of the peptide bond. Stacking interactions between proline rings and phenol rings, that is CH⋯π hydrogen bonds, also stabilize the dynamic structure of the complex.