Molecular Insights into Protein‐Polyphenols Aggregation: A Dynamic and Topological Description

Abstract Protein‐polyphenols interactions are of greatest interest in several fields like food technology and leather industry. Also, it is thought that these interactions are responsible for the undesired phenomenon of colloidal turbidity. However, there is sparse information about the molecular implications leading to this phenomenon. In this study, Molecular Dynamic (MD) simulations in conjunction with the analysis of the topology of the electron density are used to study protein/polyphenol interactions in a model system which consists of a ternary mixture of water, the flavonoids Catechin and Procianidin B3 and proline pentapeptides. After 50 ns of simulation, root mean square deviation, root mean square fluctuation and number of hydrogen bonds were calculated. Information about the intermolecular interactions that drive the assembly of colloidal complexes has been obtained by the analysis of the electron charge density. Results show the formation of a stable adduct, with a very complex network of conventional and non‐conventional hydrogen bonds. This study has also shown the significance of C‐H⋅⋅⋅O and C‐H⋅⋅⋅π interactions in the phenomenon of colloidal turbidity.