Isolation, Characterization, and Single-Crystal X‑ray\nAnalysis of Lantabetulic Acid from Rhus alata: Insights into HSA and BSA Binding Interactions, with In-Silico\nStudy

This study investigated\nthe bioactive potential of Rhus alata, a plant known for its rich phytochemicals.\nA previously unreported compound was isolated from R. alata and characterized using various spectroscopic\ntechniques (IR, UV, NMR, MS) and confirmed for the first time by X-ray\ncrystallography. In isolated compound 1, noncovalent interactions\nbetween H···H/H···H, C···C/C···C\nand O···H/H···O play a major role in\nits packing arrangement. This observation is consistent with the results\nof Hirshfeld surface analysis, which quantified these interactions\nas 14.2%, 84.6%, and 1.2%, respectively. The isolated compound was\nidentified as lantabetulic acid (<b>1</b>) (3β,25-expoxy-3α-hydroxylup-20(29)-en-28-oic\nacid). To understand its potential biological interactions, the binding\naffinity of lantabetulic acid to biomolecules such as bovine serum\nalbumin (BSA), and human serum albumin (HSA), was assessed. The results\nshowed significant binding efficacy, indicating potential interactions\nwith these molecules. Furthermore, the DPPH assay demonstrated the\npotent antioxidant activity of this compound. We used in silico molecular\ndocking to clarify the binding affinity between lantabetulic acid\nand a particular receptor. Furthermore, molecular dynamic simulation\nstudies also explored the binding interaction. As well, MM/GBSA calculations\ncorroborate the simulation results and the stability of the complex.\nDocking and dynamics studies revealed promising binding scores, suggesting\nfurther investigation into their potential therapeutic applications.\nGeometric parameters and the absorption spectrum of compound 1 were\nalso determined using the DFT approach and compared with experimental\nfindings.