Spectroscopic and in silico characterization of the interaction between synthetic 2-substituted-naphtho-1,4-quinones and human serum albumin

圆二色性 人血清白蛋白 色氨酸 氢键 化学 荧光 对接(动物) 疏水效应 结晶学 猝灭(荧光) 滴定法 立体化学 结合常数 生物化学 有机化学 结合位点 分子 氨基酸 物理 护理部 医学 量子力学
作者
Micaeli Louise da Silva Moreira,Otávio Augusto Chaves,Nanci C. de Lucas,Juliana da Silva Goulart,Simon J. Garden,Carlos Serpa,José Carlos Netto‐Ferreira
出处
期刊:Journal of Molecular Liquids [Elsevier BV]
卷期号:403: 124829-124829 被引量:18
标识
DOI:10.1016/j.molliq.2024.124829
摘要

The intermolecular interaction between 2-(N-phenyl-N-methyl)aminonaphtho-1,4-quinone (1) and 2-(4-N-methylaminophenyl)naphtho-1,4-quinone (2) and human serum albumin (HSA) was investigated using spectroscopic techniques combined with in silico calculations via molecular docking. Steady-state titration of HSA fluorescence by 1 and 2 (λexc 295 nm) in PBS at 305, 310, and 315 K, as well as studies employing time-resolved fluorescence emission, demonstrated that the HSA:1 and HSA:2 interaction occurs through a static quenching mechanism. The Stern-Volmer constant (Ksv) values, (1.56 ± 0.08) and (3.05 ± 0.10) × 104 L/mol at 310 K for HSA:1 and HSA:2, respectively, indicate a moderate binding affinity. Van't Hoff plots showed that HSA:1 and HSA:2 interactions are spontaneous (negative ΔGo) with a hydrophobic character (ΔSo value of 0.00707 ± 0.00106 and 0.0392 ± 0.0062 kJ/mol K for HSA:1 and HSA:2, respectively) and specific electrostatic interactions (ΔHo value of –22.7 ± 3.3 and −14.4 ± 1.9 kJ/mol for HSA:1 and HSA:2, respectively). Synchronous fluorescence results showed significant perturbation in the microenvironment of the tryptophan residue (Trp-214). Circular dichroism indicated that after interaction with naphthoquinones 1 and 2, the HSA structure remains predominantly in the α-helix form. Finally, molecular docking revealed the formation of hydrophobic, electrostatic, and hydrogen bond interactions with the surrounding amino acid residues in subdomain IIA of HSA, which contains the Trp-214 residue, validated with the experimental drug-displacement assays. Overall, spectroscopic and in silico characterization of HSA:1 and HSA:2 might reflect in a low half-life in the human bloodstream, indicating the necessity of methods to improve the bioavailability, e.g., studies on the type of administration (oral versus intravenous).
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