Repaglinide (RPG) regulates the amount of glucose by stimulating the pancreas to release insulin in the blood. In view of its biological importance, we have examined the interaction between RPG and a model protein, bovine serum albumin (BSA) employing various spectroscopic, electrochemical and molecular docking methods. Fluorescence spectra of BSA were recorded in the presence and absence of RPG in phosphate buffer of pH 7.4. Fluorescence intensity of BSA was decreased upon the addition of increased concentrations of RPG, indicating the interaction between RPG and BSA. Stern-Volmer quenching analysis results revealed that RPG quenched the intensity of BSA through dynamic quenching mechanism. This was further confirmed from the time-resolved fluorescence measurements. The binding constant as calculated from the spectroscopic and voltammetric results was observed to be in the order of 10⁴ M⁻¹ at 298 K, suggesting the moderate binding affinity between RPG and BSA. Competitive experimental results revealed that the primary binding site for RPG on BSA was site II. Absorption and circular dichroism studies indicated the changes in the secondary structure of BSA upon its interaction with RPG. Molecular simulation studies pointed out that RPG was bound to BSA in the hydrophobic pocket of site II.

瑞格列奈（RPG）通过刺激胰腺在血液中释放胰岛素来调节葡萄糖的含量。考虑到其生物学重要性，我们使用各种光谱，电化学和分子对接方法研究了RPG与模型蛋白，牛血清白蛋白（BSA）之间的相互作用。在pH 7.4的磷酸盐缓冲液中有无RPG的情况下记录BSA的荧光光谱。加入增加浓度的RPG会降低BSA的荧光强度，表明RPG和BSA之间存在相互作用。Stern-Volmer猝灭分析结果表明，RPG通过动态猝灭机理猝灭了BSA的强度。时间分辨荧光测量进一步证实了这一点。 在298 K处为⁴  M ^-1，表明RPG和BSA之间具有中等结合亲和力。竞争性实验结果表明，BSA上RPG的主要结合位点是位点II。吸收和圆二色性研究表明，BSA与RPG相互作用后，其二级结构发生了变化。分子模拟研究指出，RPG在位点II的疏水口袋中与BSA结合。