Antimicrobial peptides from C-terminal amphipathic region of E. coli FtsA

Publication date: Available online 15 September 2018Source: Biochimica et Biophysica Acta (BBA) - BiomembranesAuthor(s): Karabi Saikia, Nitin ChaudharyAbstractAntimicrobial peptides constitute an indispensable component of innate immune system in organisms ranging from bacteria to man. Despite this, peptides lag far behind the conventional antibiotics in treating infections. The menace of multidrug-resistant bacteria, however, has revived the antimicrobial peptide research. We reasoned that the membrane-binding regions of bacterial proteins could be purposed to combat them. Here, we identify potent antimicrobial peptides from the C-terminal amphipathic helix of E. coli FtsA protein. The 11 and 13-residue peptides exhibited activity against E. coli, gentamicin-resistant MRSA, and C. albicans. The activity is little affected by the presence of salt and divalent cations. The peptides preferentially bind to the negatively-charged membranes as indicated by tryptophan fluorescence studies. The peptides permeabilize the E. coli outer and inner membranes at very promising concentrations suggesting membrane-disruption as one of the mechanisms of killing.Graphical abstract
Source: Biochimica et Biophysica Acta (BBA) Biomembranes - Category: Biochemistry Source Type: research