Binding interactions of hematoporphyrin monomethyl ether with human serum albumin

The binding of HMME derivative to human serum albumin(HSA) in aqueous solution was studied using fluorescence spectra and absorption spectra. It was shown that HMME has a powerful ability to quench the HSA fluorescence by a non-radiative energy transfer mechanism. The binding constant K were obtained by fluorescence quenching method. The quenching mechanism of fluorescence of HSA by HMME is a static quenching procedure The critical binding distance R-0 and the energy transfer efficiency E were calculated based on the theory of Foster spectroscopy energy transfer. The binding power is mainly the hydrophobic forces according to the thermodynamic parameters.