Bovine Serum Albumin Interaction with Glycyrrhizin Studiedby UV-Vis Spectroscopy and Molecular Docking
Publish place: the seventh International Conference on Technology Development in Chemical Engineering
Publish Year: 1402
نوع سند: مقاله کنفرانسی
زبان: English
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شناسه ملی سند علمی:
CHEMISB07_026
تاریخ نمایه سازی: 7 تیر 1403
Abstract:
In this research, the interaction of glycyrrhizin (GL) with bovine serum albumin (BSA) has beeninvestigated by UV–Visible spectroscopy and molecular docking simulation. The UV–visible spectroscopicmethod and molecular modeling were performed to determine the binding constant and the binding structureof the GL-BSA complex, respectively. The results of UV–visible spectroscopy showed that GL bonded to BSAwith a binding constant of KGL-BSA = ۴۹.۴ (۹۰۹۰.) × ۱۰۴Lmol-۱. The results of molecular docking revealeda minimized affinity value for the first pose of GL-BSA, which was -۱۱۹۲.kcalmol-۱, and four amino acids(Tyr۱۵۶, Thr۱۸۳, Lys۱۸۴, and Ala۲.۰) exhibited high affinity with GL. The GL-BSA complex primarilyforms based on hydrogen bonds.
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Authors
Firouzeh Manouchehri
Department of Chemistry, Central Tehran Branch, Islamic Azad University, Tehran, Iran
Ehteram Tajik
Department of Biology, Science and Research Branch, Islamic Azad University, Tehran, Iran