Theoretical affinity order among flavonoids and amino acid residues: An approach to understand flavonoid-protein interactions

The theoretical affinity order previously suggested for the interactions of flavanol species with the 20 amino acid residues was strengthened by different ways: the analysis of the PDB data about the interactions of proteins with flavonoids, the references related with the inhibition of enzymes by flavonoids and the results of docking calculations. The results confirmed that hydrophilic amino acid residues demonstrated high affinity interacting with flavonoid molecules, as it was predicted by the theoretical affinity order. The docking modes among catechin molecules and four proteins (human serum albumin (HSA), transtyretine, elastase and renin) are also supporting this information. The theoretical affinity order among flavonoids and amino acid residues seems to have great applications to the theoretical prediction of flavonoid-protein interactions as a good approach to understand the biological activity of flavonoids.