چکیده مقاله
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 = 49 4 9090 × 104Lmol 1 The results of molecular docking revealeda minimized affinity value for the first pose of GL BSA, which was 1192 kcalmol 1, and four amino acids Tyr156, Thr183, Lys184, and Ala2 0 exhibited high affinity with GL The GL BSA complex primarilyforms based on hydrogen bonds
کلیدواژهها
نویسندگان
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
شیوه ارجاع
Manouchehri, Firouzeh and Tajik, Ehteram,1402,Bovine Serum Albumin Interaction with Glycyrrhizin Studiedby UV-Vis Spectroscopy and Molecular Docking,the seventh International Conference on Technology Development in Chemical Engineering,Tehran
ارائهشده در
مجموعه مقالات هفتمین کنفرانس بین المللی توسعه فناوری در مهندسی شیمی30 بهمن 1402 · تهران