Pseudo-phase portrait applied to pattern recognition in flavonoid-protein interactions

Pattern recognition represents an attractive scientific field in the study of biological interactions. The interactions between flavonoids and proteins are extremely important in the explanation of the biological activity of these compounds. In this paper, the geometrical morphology of pseudo-phase portrait of the primary sequence of several proteins is evaluated, in order to have an approach to the pattern recognition in flavonoid-protein interactions. The theoretical affinity order (TAO) among flavonoids and amino acids residues of proteins is additionally applied in order to reduce the protein sequence complexity by residue grouping. The high potentiality of pseudo-phase portrait, as a qualitative descriptor is shown. Its morphology suffers significant modifications as a function of the analyzed protein sequences and therefore it becomes an important indicator or a characteristic pattern of flavonoid-protein interactions. It could be a useful application in the prediction of potential proteins to interact with flavonoid molecules.