Evaluating Taniborbactam as an Inhibitor of the SDS-Hydrolyzing Enzyme SdsA1 via Structural and Docking Analysis

Pseudomonas aeruginosa is a major cause of hospital-acquired infections, demonstrating remarkable resilience against standard disinfectants such as sodium dodecyl sulfate (SDS). This study investigates the potential inhibition of the SDS-hydrolyzing enzyme SdsA1 using taniborbactam, a broad-spectrum metallo-β-lactamase inhibitor. Structural alignment of SdsA1 with IMP-1 revealed strong spatial conservation, particularly around the binuclear zinc-binding motifs. Sequence alignment further identified shared zinc-coordinating motifs despite low global sequence identity. Molecular docking of taniborbactam predicted strong binding affinities at the catalytic site of SdsA1, supporting the feasibility of enzymatic inhibition. These findings suggest that repurposing taniborbactam may enhance disinfection strategies by preventing SDS degradation and reducing pathogen persistence in healthcare environments.