In Silico Docking Analysis of Peptide Deformylase (PDF) - A Novel Target for Prophylaxis of Leptospirosis

Abstract

Peptide deformylase (PDF) is a metalloproteinase and executes an essential step in the maturation of proteins in eubacteria, by removing the formyl group from the N-terminal methionine residue of ribosome-synthesized polypeptides. This process is crucial for bacterial survival because mature proteins do not retain N-formyl-methionine, and all known N-terminal peptidases cannot utilize formylated peptides as substrate. Thus, inhibition of PDF is essential to obstruct the bacterial protein maturation process. Antibiotics based on PDF inhibition have the potential to provide the much needed antibacterial activity against most of the major drug-resistant pathogens. This study comprises an implementation of in-silico techniques to validate and map the features of the respective active site of PDF from Leptospira interrogans. Our analysis consolidates PDF as a promising target for developing novel alternatives as well as indicates superior affinity of current therapeutic agents towards it. This consequently provides a new insight for leptospirosis treatment.