Probing the binding of vitexin to human serum albumin by multispectroscopic techniques

► We investigate the binding mechanism of vitexin to human serum albumin (HSA) by different multi-spectroscopic techniques under simulated physiological conditions. ► Vitexin can strongly quench the fluorescence of HSA through a static quenching mechanism. ► The interaction of vitexin with HSA is driven mainly by hydrogen bond and van der Waals forces. ► The binding distance between HSA and vitexin is 4.16 nm, and vitexin is mainly located in the region of site I (subdomain IIA). ► The binding of vitexin to HSA can induce conformational changes of HSA.