Publication: Biophysical insight into the interaction mechanism of 4-bromo-N-(thiazol-2-yl)benzenesulfonamide and human serum albumin using multi-spectroscopic and computational studies
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Issued Date
2025-01-01
Resource Type
ISSN
09280987
eISSN
18790720
Scopus ID
2-s2.0-85209397063
Pubmed ID
39528098
Journal Title
European Journal of Pharmaceutical Sciences
Volume
204
Rights Holder(s)
SCOPUS
Bibliographic Citation
European Journal of Pharmaceutical Sciences Vol.204 (2025)
Suggested Citation
Ayimbila F., Phopin K., Ruankham W., Pingaew R., Prachayasittikul S., Prachayasittikul V., Tantimongcolwat T. Biophysical insight into the interaction mechanism of 4-bromo-N-(thiazol-2-yl)benzenesulfonamide and human serum albumin using multi-spectroscopic and computational studies. European Journal of Pharmaceutical Sciences Vol.204 (2025). doi:10.1016/j.ejps.2024.106961 Retrieved from: https://hdl.handle.net/20.500.14740/20909
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Abstract
4-Bromo-N-(thiazol-2-yl)benzenesulfonamide (1) is enriched with bioactive components and is highlighted for its pharmacological properties. However, its pharmacokinetic characteristics are yet to be reported. The interaction of compound 1 with carrier proteins in the bloodstream is an important factor that affects its potential therapeutic efficacy. This study aimed to elucidate the pharmacokinetic mechanisms of compound 1 in relation to human serum albumin (HSA) using multi-spectroscopic and computational techniques. Its predicted drug-like properties revealed no mutagenicity, although potential hepatotoxicity and interactions with certain cytochrome P450 enzymes were observed. Spectroscopic analyses extensively provided the interaction between HSA and 1 through a static fluorescence quenching mechanism with spontaneous hydrophobic interactions and hydrogen bonding. The binding constant of the HSA‒1 complex was relatively moderate to strong at a level of 106 M−1. Various spectroscopic techniques including ultraviolet-visible, Fourier transform infrared, and circular dichroism spectroscopies indicated that its binding induced alteration in the α-helix content of HSA. Competitive binding and molecular docking studies designated the preferential binding of 1 to sub-structural domain IIA binding site I of HSA. Molecular dynamic simulations further illustrated the formation of a stable complex between 1 and HSA, accompanied by conformational changes in the protein. Importantly, esterase capacity of the HSA‒1 complex increased compared to the free HSA. Therefore, elucidation of the HSA‒1 binding mechanism provides valuable insights into the pharmacokinetics, suggesting potential benefits for the further development of 1 as a therapeutic agent.