Molecular Docking Analysis of Bioactive Compounds from Wurfbainia compacta Against Candida albicans Virulence Proteins

Candida albicans is an opportunistic pathogen that causes oral and systemic candidiasis, especially in immunocompromised individuals. Natural medicines obtained from medicinal plants offer compelling alternatives for addressing virulence factors in C. albicans, including adhesins and enzymes secreted for biofilm development. This study examined molecular docking (using AutoDock Vina software) to test and evaluate the binding affinities of four natural compounds—2,7-Dioxa-tricyclo[4.4.0.0(3,8)]deca-4,9-diene, dodecanoic acid 2,3-bis(acetyloxy)propyl ester, hexadecanoic acid ethyl ester, and ethyl iso-allocholate—against the virulence proteins ALS1, ALS3, SAP4, SAP5, and SAP6 of C. albicans. Docking and physicochemical, pharmacokinetic, and toxicity assessments were conducted to ascertain their potential as antifungal drugs. Ethyl iso-allocholate exhibited the highest binding affinity, especially towards SAP6 (− 8.4 kcal/mol), suggesting that is a promising antifungal agent. Among the tested compounds, ethyl iso-allocholate demonstrated the strongest and most consistent binding interactions with key virulence proteins of C. albicans, particularly SAP6, indicating its potential as a promising lead molecule for the development of novel antifungal therapeutics targeting pathogenic mechanisms.