Mechanistic insights on the antibiofilm potential of snake venom peptides: An in silico based molecular docking approach

Abstract

The threat of antibiotic resistance to the public's health is exacerbated by the emergence of multidrug resistant bacterial (MDR) strains and their biofilm. Antibiotics are unable to penetrate the thick biofilm matrix causing the indwelling bacterial cells to survive resulting into the origin of antimicrobial resistance (AMR). Thus, biofilms are responsible for causing many chronic infections such as dental plaque formation, cystic fibrosis, urinary tract infections (UTI), otitis media etc. Hence, there is an urgent need for alternate therapeutic strategies for preventing bacterial biofilm formation and fighting AMR. In this regard antimicrobial peptides (AMPs) that have broad-spectrum antibacterial action with significant specificity and low toxicity, are a great choice to combat AMR. Peptides derived from snake venom such as cathelicidins reflects a spectrum of biological actions including its antimicrobial potential. The present study focuses on screening and identifying AMPs having anti-biofilm properties. This includes natural cathelicidins found in snake venom as a potential antibacterial agent to combat AMR. Two biofilm forming proteins were identified viz. icaC protein of Staphylococcus aureus & bdlA protein of Pseudomonus aureginosa. AMPs were screened from DRAMP Database and snake venom cathelicidins were selected for further studies. The binding interaction of cathelicidins with the icaC and bdlA protein were investigated using molecular docking studies. Based on the interacting amino acid residues, antigenic determinants, peptide binding site and docking scores a performance scale was built to classify relevant snake venom cathelicidins according to their importance for further in vivo and in vitro antibiofilm investigations.