【摘要】 用光谱方法研究人血清白蛋白(HSA)与头孢哌酮(CPZ)分子间结合作用机制,头孢哌酮与β内酰胺酶的亲和力。由LineweaveBurk双倒数作图法确定了该反应的解离常数(15℃)Kd=1.10×10-4,(37℃)Kd=0.85×10-4。依据Frster非辐射能量转移机制,得到给体受体间的结合距离和能量转移效率;确定了头孢哌酮与人血清白蛋白以静电作用为主。认为头孢哌酮对β内酰胺酶稳定性与药物结构有关;抗菌活性和抗生素效力与能量转移效率和解离常数有关。同步荧光技术考察头孢哌酮对人血清蛋白构象的影响。更多还原

【Abstract】 The reaction mechanism between cefoperazone and human serum albumin(HSA) and the affinity between cefoperazone and β-lactamase were investigated by spectrometry and spectrofluorimetry. The interaction dissociation constants of human serum albumin and cefoperazone have been determined from a double reciprocal Lineweaver-Burk plot. The binding distance and the transfer efficiency between cefoperazone and HSA were also obtained according to the theory of Frster’ non-radiation energy transfer. The result suggested that the main binding force between cefoperazone and HSA is electrostatic force interaction. The high β-lactamase stability of cefoperazone may be correlative with its molecular structure. The antibiotic activity and valency connect with transfer efficiency and dissociation constant. The effect of cefoperazone on the conformation of HSA was also analyzed using synchronous fluorescence spectrometry.更多还原