Highly potent antimicrobial peptides from N-terminal membrane-binding region of E. coli MreB.

ABSTRACT: Microbial pathogenesis is a serious health concern. The threat escalates as the existing conventional antimicrobials are losing their efficacy against the evolving pathogens. Peptides hold promise to be developed into next-generation antibiotics. Antimicrobial peptides adopt amphipathic structures that could selectively bind to and disrupt the microbial membranes. Interaction of proteins with membranes is central to all living systems and we reasoned that the membrane-binding domains in microbial proteins could be developed into efficient antimicrobials. This is an interesting approach as self-like sequences could elude the microbial strategies of degrading the antimicrobial peptides, one of the mechanisms of showing resistance to antimicrobials. We selected the 9-residue-long membrane-bin

SUBMITTER: Saikia K 

PROVIDER: S-EPMC5322399 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature