How hydrophilic group affects drug–protein binding modes: Differences in interaction between sirtuins inhibitors Tenovin-1/Tenovin-6 and human serum albumin

Na Gan,Qiaomei Sun,Zili Suo,Shuangshuang Zhang,Ludan Zhao,Hongzhao Xiang,Wenjing Wang,Zhiqiang Li,Xiaoxiang Liao,Hui Li

Journal of Pharmaceutical and Biomedical Analysis（2021）

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摘要

•The hydrophilic group of T6 decreased the binding constant compared with T1.•HSA in the T6 system undergo a more significant conformational transition.•T1 and T6 quenched the endogenous fluorescence of HSA via static mechanism.•Both systems were spontaneous reactions driven by hydrophobic interaction.

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关键词

Human serum albumin,Sirtuin inhibitor,Interaction

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