Unicentric Castleman's disease with leiomyosarcoma: a rare association.

UNLABELLED: Diabetes mellitus is a chronic metabolic disorder characterized by persistent hyperglycemia. Ficus racemosa is a widely used ethnomedicinal plant with known antidiabetic and antioxidant properties. The present study investigated the antidiabetic potential of the plant using LC-MS-based phytochemical profiling, molecular docking, molecular dynamics simulation (MDS), and MM-PBSA analysis. LC-MS analysis of the diethyl ether extract of F. racemosa identified 56 bioactive compounds. Molecular docking analysis showed phytocompound usambarensine as the best-performing ligand against both α-amylase (- 10.8 kcal/mol) and α-glucosidase (- 9.6 kcal/mol). van der Waals interactions were the most predominant forces contributing to protein-ligand binding, followed by H-bonds. MDS was performed to investigate the stability and interaction dynamics of α-amylase and α-glucosidase complexes with the test ligand and the reference inhibitor acarbose. Docking results indicated comparatively higher predicted binding affinities for the test ligand (- 10.8 and - 9.6 kcal/mol) than acarbose (- 8.1 and - 7.2 kcal/mol) against α-amylase and α-glucosidase, respectively. However, MDS suggested comparatively greater dynamic stability for the acarbose complexes. RMSD and RMSF analyses indicated higher structural flexibility in the apo proteins, whereas ligand-bound systems exhibited reduced fluctuations, suggesting ligand-induced stabilization. The radius of gyration remained stable throughout the simulation, indicating preserved structural compactness of the enzymes. H-bond and H-bond occupancy analyses demonstrated persistent interactions with favorable donor-acceptor geometry. Furthermore, principal component analysis revealed broader conformational sampling in apo proteins and more compact clusters in ligand-bound complexes. Center-of-mass analysis also confirmed stable ligand-enzyme interactions. Overall, the results suggest potential stable interactions between the phytocompound and both target enzymes.

SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1007/s40203-026-00703-7.