Interaction of MreB-derived antimicrobial peptides with membranes

Biochemical and Biophysical Research Communications
Karabi Saikia, Nitin Chaudhary

Abstract

Antimicrobial peptides are critical components of defense systems in living forms. The activity is conferred largely by the selective membrane-permeabilizing ability. In our earlier work, we derived potent antimicrobial peptides from the 9-residue long, N-terminal amphipathic helix of E. coli MreB protein. The peptides display broad-spectrum activity, killing not only Gram-positive and Gram-negative bacteria but opportunistic fungus, Candida albicans as well. These results proved that membrane-binding stretches of bacterial proteins could turn out to be self-harming when applied from outside. Here, we studied the membrane-binding and membrane-perturbing potential of these peptides. Steady-state tryptophan fluorescence studies with tryptophan extended peptides, WMreB1-9and its N-terminal acetylated analog, Ac-WMreB1-9show preferential binding to negatively-charged liposomes. Both the peptides cause permeabilization of E. coli inner and outer-membranes. Tryptophan-lacking peptides, though permeabilize the outer-membrane efficiently, little permeabilization of the inner-membrane is observed. These data attest membrane-destabilization as the mechanism of rapid bacterial killing. This study is expected to motivate the research in id...Continue Reading

References

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Feb 24, 2017·Scientific Reports·Karabi SaikiaNitin Chaudhary

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Citations

Jan 28, 2021·The Journal of Antimicrobial Chemotherapy·Mário R FelícioSónia Gonçalves
Jan 25, 2020·Biochimie·Sathishkumar MunusamyCarlos Munoz-Garay
Sep 15, 2019·Biochemical and Biophysical Research Communications·Karabi SaikiaNitin Chaudhary
Jun 13, 2021·Biophysical Chemistry·Anshuman MohapatraNitin Chaudhary
Mar 12, 2020·ACS Infectious Diseases·Declan Alan Gray, Michaela Wenzel

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