1. College of Bioengineering, Dalian University, Dalian 116622, China 2. Liaoning Key Lab of Bio-organic Chemistry, Dalian University, Dalian 116622, China 3. College of Environment and Chemical Engineering, Dalian 116622, China
Abstract:The interaction between vincristine (VCR) and bovine serum albumin (BSA) was investigated by UV-Vis absorption, fluorescence and circular dichroism (CD) spectra at 296, 303 and 310 K, respectively. With fluorescence quenching method, the binding constants Ka were determined to be 1.5×104 L·mol-1, 9.5×103 L·mol-1, 4.9×103 L·mol-1 and the number of binding site was 1 at three temperatures, respectively. The conformation of BSA was altered (CD data) with the reductions of α-helices from 33.5% for free BSA to 29.7%, and with increases of β-sheet from 13.6% for free BSA to 18.4% in the presence of VCR. The thermodynamic parameters, enthalpy change (ΔH) and entropy change (ΔS), were calculated to be -62.07 kJ·mol-1 and -129.38 J·(mol·K)-1 respectively, according to van′t Hoff equation, which indicated that hydrogen bonds and van der walls interactions played major roles in the binding process.
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