The interaction of four benzothiazole tethered triazole analogues (MS43, MS70, MS71, and MS78) with human serum albumin (HSA) was investigated using various spectroscopic techniques (ultraviolet-visible (UV-vis) light absorption, fluorescence, circular dichroism (CD), molecular docking and density functional theory (DFT) studies). Fluorescence quenching constants (~1012 ) revealed a static mode of quenching and binding constants (Kb ~104 ) indicating the strong affinity of these analogues for HSA. Further alteration in the secondary structure of HSA in the presence of these analogues was also confirmed by far UV-CD spectroscopy. The intensity loss in CD studied at 222 nm indicated an increase in random coil/β-sheet conformations in the protein. Binding energy values (MS71 (-9.3 kcal mol-1 ), MS78 (-8.02 kcal mol-1 ), MS70 (-7.16 kcal mol-1 ) and MS43 (-6.81 kcal mol-1 )) obtained from molecular docking revealed binding of these analogues with HSA. Molecular docking and DFT studies validated the experimental results, as these four analogues bind with HSA at site II through hydrogen bonding and hydrophobic interactions.

中文翻译：

---

深入了解苯并噻唑系留的三唑类似物与人血清白蛋白的相互作用：光谱学和分子对接方法。

使用各种光谱技术（紫外可见（UV-vis）光吸收，荧光，圆二色性（CD））研究了四种苯并噻唑系留的三唑类似物（MS43，MS70，MS71和MS78）与人血清白蛋白（HSA）的相互作用。 ，分子对接和密度泛函理论（DFT）研究）。荧光猝灭常数（〜1012）显示了猝灭和结合常数（Kb〜104）的静态模式，表明这些类似物对HSA具有很强的亲和力。在存在这些类似物的情况下，HSA二级结构的进一步改变也通过远紫外-CD光谱法得到了证实。在222 nm处研究的CD中的强度损失表明该蛋白质中的无规卷曲/β-折叠构象增加。结合能值（MS71（-9.3 kcal mol-1），MS78（-8.02 kcal mol-1），MS70（-7。从分子对接获得的16kcal mol-1）和MS43（-6.81 kcal mol-1））揭示了这些类似物与HSA的结合。分子对接和DFT研究验证了实验结果，因为这四个类似物通过氢键和疏水作用与II位的HSA结合。