一种多技术方法探讨治疗性酪氨酸激酶抑制剂尼达尼布和牛血清白蛋白的相互作用

A. Abdelhameed, S. Nusrat, S. Paliwal, M. Zaman, Nida Zaidi, R. H. Khan
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引用次数: 7

摘要

药物与蛋白质的相互作用为合理设计药物、合成更有效的新药和改良药物提供了结构指导。本文用光谱技术研究了抗癌药物(酪氨酸激酶抑制剂)尼达尼布(NTB)与牛血清白蛋白(BSA)的相互作用趋势和机制。Stern-Volmer猝灭常数和结合常数随温度升高而降低,表明BSA与NTB形成配合物。通过修正Stern-Volmer方程得到的3种温度下的结合常数约为~104 M−1。负的ΔG(~−5.93 kcal mol−1)、ΔH(−3.74 kcal mol−1)和ΔS(−1.50 kcal mol−1)值表明BSA与NTB发生自发放热反应。荧光结果表明,NTB分子通过形成氢键与BSA相互作用。此外,圆二色光谱还观察到牛血清白蛋白与NTB结合后螺旋构象有微小的增加。动态光散射测量结果表明,NTB存在时,蛋白质的对称性发生改变,流体动力半径减小(从~3.6 nm到~3 nm)。图形抽象
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A multitechnique approach to probe the interaction of a therapeutic tyrosine kinase inhibitor nintedanib and bovine serum albumin
ABSTRACT Drug and protein interaction provides a structural guideline in the rational drug designing and in the synthesis of new and improved drugs with greater efficacy. We have examined here the interaction tendency and mechanism of nintedanib (NTB), an anticancer drug (tyrosine kinase inhibitor) with bovine serum albumin (BSA), by spectroscopic techniques. The decline in Stern–Volmer quenching constants and binding constant with the temperature rise suggests that BSA forms a complex with NTB. Binding constant obtained by modified Stern–Volmer equation at 3 temperatures was realized to be of the order of ~104 M−1. Negative ΔG (~−5.93 kcal mol−1), ΔH (−3.74 kcal mol−1), and ΔS (−1.50 kcal mol−1) values exhibited a spontaneous and exothermic reaction between BSA and NTB. NTB molecule interacts with BSA by forming hydrogen bonds, as elucidated by fluorescence results. Moreover, a minor increment in the helical conformation of BSA upon its binding to NTB was observed by circular dichroism spectroscopy. The modification in protein’s symmetry and a decline in hydrodynamic radii were observed in the presence of NTB (from ~3.6 to ~3 nm) as obtained by the dynamic light scattering measurement results. GRAPHICAL ABSTRACT
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