Human serum albumin (HSA), one of the most copious plasma proteins is responsible for binding and transportation of many exogenous and endogenous ligands including drugs. In this study, we intended to explore the extent and types of binding interaction present between HSA and the antihypertensive drug, telmisartan (TLM). The conformational changes in HSA due to this binding were also studied using different spectroscopic and molecular docking techniques. The spectral shifting and intensity variations upon interaction with TLM were studied using FT-IR spectroscopy. Binding constant and the change in absorption of HSA at its λ_max was analyzed using absorption spectroscopy. Eventually, the types and extent of binding interactions were confirmed using molecular docking technique. Results have shown that TLM significantly interacts with the binding site-1 of HSA utilizing strong hydrogen bonding with Glu292, and Lys195 residues. The UV-absorption intensities were found to be decreased serially as the drug concentration increased with a binding constant of 1.01 × 10³ M⁻¹. The secondary structure analysis using FT-IR spectroscopy also revealed a marked reduction in the α-helix (56%) component of HSA on interaction. This study gives critical insights into the interaction of TLM with HSA protein which eventually affects the concentration of TLM reaching the site of action and ultimately its therapeutic profile.

人血清白蛋白 (HSA) 是最丰富的血浆蛋白之一，负责结合和运输许多外源性和内源性配体，包括药物。在这项研究中，我们打算探讨 HSA 与抗高血压药物替米沙坦 (TLM) 之间存在的结合相互作用的程度和类型。还使用不同的光谱和分子对接技术研究了由于这种结合导致的 HSA 构象变化。使用 FT-IR 光谱研究了与 TLM 相互作用时的光谱偏移和强度变化。结合常数和 HSA 在其 λ _{max处的吸收变化}使用吸收光谱进行分析。最终，使用分子对接技术确认了结合相互作用的类型和程度。结果表明，TLM 利用与 Glu292 和 Lys195 残基的强氢键与 HSA 的结合位点 1 显着相互作用。发现随着药物浓度的增加，紫外吸收强度连续降低，结合常数为 1.01 × 10 ³ M ^-1。使用 FT-IR 光谱的二级结构分析还显示，HSA 的 α-螺旋 (56%) 组分在相互作用时显着减少。这项研究对 TLM 与 HSA 蛋白的相互作用提供了重要的见解，最终影响 TLM 到达作用部位的浓度并最终影响其治疗概况。