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利用荧光光谱法研究缬沙坦与人血清白蛋白的作用机制。判断出缬沙坦对人血清白蛋白(HSA)体系的猝灭是由于生成复合物的静态猝灭,计算出在30℃缬沙坦与HSA相互作用的结合位点数和结合常数分别为n30℃=0.53和K30℃=761.8,37℃时缬沙坦与HSA相互作用的结合位点数和结合常数分别为n37℃=0.48和K37℃=374.8。此外,还得出了一些金属离子存在下的结合常数(KCa=3899.5,KCu=1081.4,KFe=1595.1,KZn=3833.6)。体系的热力学常数分别为ΔH=-24.9kJ/mol,ΔS30℃=38.2J.mol-1.K-1,ΔS37℃=34.5J.mol-1.K-1,由此得出缬沙坦与人血清白蛋白之间是以静电作用力相结合。由Frster非辐射能量转移理论计算出两者间的作用距离r=2.07nm。并利用同步荧光技术,考察了缬沙坦对蛋白质构象的影响。
Study on Mechanism of Valsartan and Human Serum Albumin by Fluorescence Spectroscopy. Judging that the quenching of human serum albumin (HSA) system by valsartan is due to the static quenching of the resulting complex, the number of binding sites and binding constants of valsartan-HSA interaction at 30 ° C. were calculated as n30 ° C. = 0.53 and K30 ℃ = 761.8, the binding sites and binding constants of valsartan-HSA interaction at 37 ℃ were n37 ℃ = 0.48 and K37 ℃ = 374.8, respectively. In addition, some binding constants (KCa = 3899.5, KCu = 1081.4, KFe = 1595.1, KZn = 3833.6) were also obtained for the presence of metal ions. The thermodynamic constants of the system are respectively ΔH = -24.9kJ / mol, ΔS30 ℃ = 38.2J.mol-1.K-1, ΔS37 ℃ = 34.5J.mol-1.K-1, Human serum albumin is based on the electrostatic force combination. Frster non-radiative energy transfer theory to calculate the role of the distance between the two r = 2.07nm. The effect of valsartan on the protein conformation was investigated by using synchronous fluorescence technique.