INDUCED CHIRALITY OF GENISTEIN UPON BINDING TO ALBUMIN: CIRCULAR DICHROISM AND TDDFT STUDY

Experimental induced circular dichroism spectra of the achiral isoflavone genistein upon binding to human serum albumin were correlated with theoretical spectra obtained by time-dependent density functional theory calculations on the neutral and three anionic species of genistein in several conformations. Coupling these methods allowed us to identify the mechanism responsible for chirality induction in genistein upon binding, namely the distortion of the molecular conformation of the ligand upon inclusion into the sterically-restricted protein binding pocket. The bound genistein species and its conformation were identified and the binding parameters were estimated.