Molecular affinity between caffeic and chlorogenic acid with proteins associated with apoptosis pathways using docking molecular analysis

Abstract

Introduction: modulation of apoptosis is necessary in the basic physiological response to cancer. However, in some cancer scenarios, apoptosis is inhibited allowing the tumor proliferation. Searching for new therapeutic agents that promote apoptosis in cancer is relevant. Among these potential agents are caffeic acid and chlorogenic acid. Several studies have evaluated the activity of polyphenols as modulators in the apoptosis process. This study evaluated the affinity of caffeic and chlorogenic acid for some proteins related with apoptosis pathway using docking molecular strategies.Methods: the pro and anti-apoptotic proteins included in the analysis were catalase, heat shock protein 27 (HSP27), P27/Kip1/CDKN, Bcl-XL, cytochrome C, PON2, H02-HM0X2, Bax. The crystallographic structures were downloaded from Protein Data Bank and ligands from PubChem. Preparation of the ligands was done in Avogadro 1.2 and proteins in Chimera 1.15. Docking experiments were implemented in Autodock Vina.Results: chorogenic acid showed the best affinity with the proposed proteins. HSP27 presented a good affinity for the two ligands, with score affinity of -7.9 in caffeic acid and -9.0 in chlorogenic acid. In the same way, catalase presented a good affinity with -7.9 in score affinity in both ligands.Conclusions: the docking molecular analysis suggests potential pro-apoptotic functions for chlorogenic and caffeic acid considering their affinity with anti-apoptotic proteins.