IN SILICO INHIBITION OF OXA-3 B-LACTAMASE BY BIOACTIVE COMPOUND IDENTIFIED IN THE LEAF OF CALITROPIS PROCERA

ABSTRACT Antibiotic resistance mediated by β-lactamases, particularly OXA-3, represents a significant clinical challenge in treating bacterial infections. This study employed molecular docking to identify and evaluate bioactive compounds from Calotropis procera leaves for their potential interactions with OXA-3 β-lactamase. Phytochemical analysis revealed the presence of multiple bioactive compound classes, including flavonoids, alkaloids, quinones, and proteins. These compounds were subjected to molecular docking studies to assess their binding affinity to OXA-3 β-lactamase and predict their inhibitory potential. Computational analysis evaluated the binding interactions of each compound with the enzyme’s active site, including binding energy calculations and key residue interactions. Drug-likeness properties and ADMET characteristics were also assessed. The molecular docking results demonstrated that flavonoids, alkaloids, and quinones exhibited favorable binding interactions with OXA-3 β-lactamase, with several compounds displaying significant binding affinities. However, despite these favorable binding predictions, the compounds did not demonstrate inhibitory activity against OXA-3 β-lactamase. These findings suggest that while bioactive compounds from Calotropis procera can interact with OXA-3 β-lactamase computationally, additional structural modifications or experimental validation may be necessary to achieve functional inhibition. This work provides a foundation for future research aimed at optimizing these natural compounds as potential antimicrobial agents and contributes to understanding the limitations of in silico predictions in drug discovery