CAJ | 학술논문

用荧光、紫外光谱、分子对接研究了柚皮苷与人血清白蛋白( HSA)在pH=7．40的Tris-HCl缓冲溶液中相互作用的情况。结果表明,柚皮苷对人血清白蛋白的内源荧光有明显的猝灭作用,猝灭过程为动态猝灭。根据Stern-Volmer方程计算得到柚皮苷与HSA 在293、298和310 K下的结合常数分别为2．472×105、2．210×105和1．392×104 L·mol-1,结合位点数约为1。由实验计算出热力学参数焓变ΔH为-16．8 kJ·mol-1,ΔS为46．0 J·mol-1·K-1,推断出柚皮苷与人血清白蛋白之间主要靠疏水作用和静电引力结合,与分子模拟的结果相同。同时采用同步荧光技术考察了柚皮苷对HSA构象的影响。
용형광、자외광보、분자대접연구료유피감여인혈청백단백( HSA)재pH=7．40적Tris-HCl완충용액중상호작용적정황。결과표명,유피감대인혈청백단백적내원형광유명현적졸멸작용,졸멸과정위동태졸멸。근거Stern-Volmer방정계산득도유피감여HSA 재293、298화310 K하적결합상수분별위2．472×105、2．210×105화1．392×104 L·mol-1,결합위점수약위1。유실험계산출열역학삼수함변ΔH위-16．8 kJ·mol-1,ΔS위46．0 J·mol-1·K-1,추단출유피감여인혈청백단백지간주요고소수작용화정전인력결합,여분자모의적결과상동。동시채용동보형광기술고찰료유피감대HSA구상적영향。
The interaction between naringin and human serum albumin(HSA)in buffer solution(pH=7. 40)were studied by fluores-cence spectroscopy,UV absorption spectroscopy,molecular modeling. It was found that naringin quenched the fluorescence of HSA via a dynamic quenching process. According to the modified Stern-Volmer equation, the binding constants between naringin and HSA at different temperatures(293,298,310 K)were 2. 47×105、2. 21×105 和1. 39×104 L·mol-1respectively,and number of bind-ing sites were 1,which indicated the strong binding between naringin and HSA. The thermodynamic parameters,enthalpy change ( ΔH ) and entropy change( ΔS ) for the reaction were calculated to be-16. 8 kJ·mol-1 and 46. 0 J·mol-1·K-1 according to van’t Hoff equation. These dates indicated that hydrophobic and electrostatic interactions played a major role in the binding of naringin and HSA,which was in good agreement with molecular modeling studies. Synchronous fluorescence spectroscopy was used in the study of the effect of naringin on the configuration of HSA.