摘要 : The interaction between whey carrier protein beta-lactoglobulin type A and B (BLG-A and -B) and 2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate (BPHDC-Pd(II)),a new heavy metal complex designed for anticancer property,was in... 展开 The interaction between whey carrier protein beta-lactoglobulin type A and B (BLG-A and -B) and 2,2'-bipyridin n-hexyl dithiocarbamato Pd(II) nitrate (BPHDC-Pd(II)),a new heavy metal complex designed for anticancer property,was investigated by fluorescence spectroscopy combined with chemometry and circular dichroism (CD) techniques.A strong fluorescence quenching reaction of BPHDC-Pd(II) to BLG-A and -B was observed.Hence,BPHDC-Pd(II) complex can be bound to both BLG-A and -B,and quench the fluorescence spectra of the proteins.The quenching constant was determined using the modified Stern-Volmer equation.The binding parameters were evaluated by fluorescence quenching method.The results of binding study provided evidences presence of two and three sets of binding sites on the BLG-B and -A,respectively,for BPHDC-Pd(II) complex.Using fluorescence spectroscopy and chemometry,the ability of BLG-A and -B to form an intermediate upon interaction with BPHDC-Pd(II) complex was assessed.CD studies displayed that under influence of different concentrations of BPHDC-Pd(II) complex,the regular secondary structure of BLG-B had no significant changes,whereas for BLG-A a transition from alpha-helix to beta-structure was appeared.The results for both of BLG-A and -B displayed that BPHDC-Pd(lT) complex can induce a conformational transition from the native form to an intermediate state with a slightly opened conformation,which is detectable with chemometry analyses. 收起