Spectroscopic investigation and structural simulation in human serum albumin with hydroxychloroquine/Silybum marianum and a possible potential COVID-19 drug candidate.

Autor: Tekyeh MSH; Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran., Shushtarian SMM; Department of Biophysics and Biochemistry, Faculty of Advance Science and Technology, Medical Sciences, Islamic Azad University, Tehran, Iran., Bakhsh AI; Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran., Tackallou SH; Department of Biology, Central Tehran Branch, Islamic Azad University, Tehran, Iran., Lanjanian H; Software Engineering Department, Engineering Faculty, Istanbul Topkapi University, Istanbul, Turkey.
Jazyk: angličtina
Zdroj: Archiv der Pharmazie [Arch Pharm (Weinheim)] 2024 Jul; Vol. 357 (7), pp. e2300751. Date of Electronic Publication: 2024 Apr 21.
DOI: 10.1002/ardp.202300751
Abstrakt: In this study, the interaction between human serum albumin (HSA) and the hydroxychloroquine/Silybum marianum (HCQ/SM) mixture was investigated using various techniques. The observed high binding constant (K b ) and Stern-Volmer quenching constant (K SV ) indicate a strong binding affinity between the HCQ/SM mixture and HSA. The circular dichroism (CD) analysis revealed that HCQ/SM induced conformational changes in the secondary structure of HSA, leading to a decrease in the α-helical content. UV-Vis analysis exhibited a slight redshift, indicating that the HCQ/SM mixture could adapt to the flexible structure of HSA. The experimental results demonstrated the significant conformational changes in HSA upon binding with HCQ/SM. Theoretical studies were carried out using molecular dynamics simulation via the Gromacs simulation package to explore insights into the drug interaction with HSA-binding sites. Furthermore, molecular docking studies demonstrated that HCQ/SM-HSA exhibited favorable docking scores with the receptor (5FUZ), suggesting a potential therapeutic relevance in combating COVID-19 with a value of -6.24 kcal mol -1 . HCQ/SM exhibited stronger interaction with both SARS-CoV-2 virus main proteases compared to favipiravir. Ultimately, the experimental data and molecular docking analysis presented in this research offer valuable insights into the pharmaceutical and biological properties of HCQ/SM mixtures when interacting with serum albumin.
(© 2024 Deutsche Pharmazeutische Gesellschaft.)
Databáze: MEDLINE
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