灯盏花乙素与α-葡萄糖苷酶相互作用的研究  

Investigation of interaction between scutellarin and α-Glucosidase

作　　者：严晓琳[1,2] 袁培耘 李欣[1] 杨庆雄[1] 

机构地区：[1]贵州师范大学化学与材料科学学院,贵州贵阳550001 [2]贵州师范大学生命科学学院,贵州贵阳550001

出　　处：《贵州师范大学学报（自然科学版）》2013年第5期79-83,共5页Journal of Guizhou Normal University：Natural Sciences

基　　金：国家自然科学基金项目资助(30860038)

摘　　要：运用酶促动力学、紫外光谱及荧光光谱研究灯盏花乙素与α-葡萄糖苷酶的相互作用,探讨灯盏花乙素对α-葡萄糖苷酶的抑制效果及抑制类型、结合类型、结合常数、结合位点数、结合过程中热力学参数以及非辐射能量转移.结果表明灯盏花艺素对α-葡萄糖苷酶的半数抑制率（IC50）为0.498mmol/L,抑制类型为非竞争性与竞争性抑制的混合型.灯盏花乙素结合α-葡萄糖苷酶内源荧光的猝灭是由于形成了新的配合物,符合静态猝灭机理.15℃℃,25℃,37℃下灯盏花乙素与α-葡萄糖苷酶的结合常数在0.99×105～1.53×105 L/mol之间,且只有1个结合位点.热力学数据表明灯盏花乙素结合α-葡萄糖苷酶之间的主要作用力是疏水作用力和氢键.F（o）rster能量转移理论确定了灯盏花乙素与α-葡萄糖苷酶的作用距离为3.97nm.The interaction between Scutellarin and α-Glucosidase were investigated using enzyme kinetics,UV spectroscopy and fluorescence spectroscopy methods.The inhibitory effect,inhibition type,binding mode,binding constants,binding sites,thermodynamic parameters between Scutellarin and α-Glucosidase,and energy transfer were studied.The experimental results showed that Scutellarin is α-Glucosidase enzyme＇sinhibitor,inhibitory modes belonged to a mixed type of noncompetitive and competitive.IC50 is 0.498mmol/L.Scutellarin had the ability to quench the intrinsic fluorescence of α-Glucosidase because of the new formed complexs,and the quenching mechanism is static quenching.Scutellarin had only one binding site on α-Glucosidase,and the binding constants were between 0.99× 105 ～ 1.53 × 105 L/mol at 15,25,37℃.The thermodynamic parmeters were calculated,which suggested that hydrophobic interaction and hydrogen bonds played a major role in the interaction.The distance and efficiency of energy transfer between Scutellarin and α-Glucosidase is 3.97nm.

关 键 词：灯盏花乙素 Α-葡萄糖苷酶 荧光光谱 紫外光谱 

分 类 号：O643.12[理学—物理化学] R977.15[理学—化学]