Journal article

The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent

MA Sani, AP Le Brun, S Rajput, T Attard, F Separovic

Biophysical Journal | CELL PRESS | Published : 2023

Abstract

Antimicrobial peptides are an important class of membrane-active peptides that can provide alternatives or complements to classic antibiotics. Among the many classes of AMPs, the histidine-rich family is of particular interest since they may induce pH-sensitive interactions with cell membranes. The AMP caerin 1.1 (Cae-1), from Australian tree frogs, has three histidine residues, and thus we studied the pH dependence of its interactions with model cell membranes. Using NMR spectroscopy and molecular dynamics simulations, we showed that Cae-1 induced greater perturbation of the lipid dynamics and water penetrations within the membrane interior in an acidic environment compared with physiologic..

View full abstract

Grants

Awarded by Australian Research Council


Funding Acknowledgements

ACKNOWLEDGMENTS This manuscript is dedicated to Dr. Klaus Gawrisch in honor of his contri-butions to membrane biophysics and NMR spectroscopy and in apprecia-tion for his many years of mentorship, encouragement, and friendship. This research was funded by the Australian Research Council (ARC) Dis-covery Project grants DP190101506 to F.S. and DP210101792 to M.-A.S. and LIEF grant LE160100120 to F.S. and M.-A.S. NMR experimentswere performed at the Bio21 Institute NMR facility and the peptide synthe-sis at the Bio21 Institute Melbourne Protein Characterization facility.