This study was conducted to examine the binding of a newly synthesized Schiff base derived from 2-hydroxy-1-naphthaldehyde and 5-amino-2-mercaptobenzimidazole with human serum albumin (HSA) employing various biophysical techniques. The thermal-based fluorescence quenching data indicated that static quenching occurred between the ligand and HSA. The fluorescence results expose that ligand quenches the intrinsic fluorescence of HSA through a static quenching procedure. The thermodynamic parameters of the binding interaction, obtained using van't Hoff equation indicated the spontaneity of the reaction. The stability of the HSA–ligand complex resulted from hydrogen bonding and hydrophobic interactions, which afforded a substantial binding affinity between ligand and HSA. UV–Vis and circular dichroism data indicated that ligand binding induced conformational changes in HSA. The energy transfer efficiency determined according to Fӧorster's theory. Absorption, distribution, metabolism, and excretion (ADME) and Lipinski’s drug likeness of the ligand was predicted, revealing that it had auspicious physicochemical properties for oral bioavailability. Furthermore, molecular modeling was also employed to determine the location of the ligand in HSA binding sites, which revealed that the ligand interacted with polar and apolar residues of site I (subdomain IIA) of HSA, predominantly through hydrophobic and hydrogen bonding interactions.

进行了这项研究，以使用各种生物物理技术检查新合成的2-羟基-1-萘醛和5-氨基-2-巯基苯并咪唑的席夫碱与人血清白蛋白（HSA）的结合。基于热的荧光猝灭数据表明，在配体和HSA之间发生了静态猝灭。荧光结果表明，配体通过静态猝灭过程猝灭了HSA的固有荧光。使用van't Hoff方程获得的结合相互作用的热力学参数表明了反应的自发性。HSA-配体复合物的稳定性来自氢键和疏水相互作用，从而在配体和HSA之间提供了显着的结合亲和力。UV-Vis和圆二色性数据表明，配体结合诱导了HSA的构象变化。能量转移效率根据Fӧorster的理论确定。预测了配体的吸收，分布，代谢和排泄（ADME）和Lipinski的药物相似性，表明该配体具有口服生物利用度的吉祥物理化学性质。此外，还通过分子建模来确定配体在HSA结合位点中的位置，这表明配体主要通过疏水和氢键相互作用与HSA的位点I（亚结构域IIA）的极性和非极性残基相互作用。可以预测该化合物的排泄和排泄（ADME）以及Lipinski的药物相似性，表明该化合物具有口服生物利用度的吉祥物理化学性质。此外，还通过分子建模来确定配体在HSA结合位点中的位置，这表明配体主要通过疏水和氢键相互作用与HSA的位点I（亚结构域IIA）的极性和非极性残基相互作用。可以预测该化合物的排泄和排泄（ADME）以及Lipinski的药物相似性，表明该化合物具有口服生物利用度的吉祥物理化学性质。此外，还通过分子建模来确定配体在HSA结合位点中的位置，这表明配体主要通过疏水和氢键相互作用与HSA的位点I（亚结构域IIA）的极性和非极性残基相互作用。