Journal article
Membrane interactions of proline-rich antimicrobial peptide, Chex1-Arg20, multimers
W Li, MA Sani, E Jamasbi, L Otvos, MA Hossain, JD Wade, F Separovic
Biochimica Et Biophysica Acta Biomembranes | Published : 2016
Abstract
The increasing prevalence of antibiotic-resistant pathogens requires the development of new antibiotics. Proline-rich antimicrobial peptides (PrAMPs), including native apidaecins, Bac7, and oncocins or designed A3APO, show multi-modal actions against pathogens together with immunostimulatory activities. The interactions of the designed PrAMP, Chex1-Arg20, and its dimeric and tetrameric oligomers with different model membranes were investigated by circular dichroism spectroscopy, dynamic light scattering, zeta potential, differential scanning calorimetry, and dye leakage. Chex1-Arg20 oligomers showed stronger affinity and preferential binding to negatively charged phospholipid bilayers and le..
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Awarded by Australian Research Council
Funding Acknowledgements
We gratefully acknowledge support of the studies undertaken in the authors' laboratory by an ARC Discovery Project grant (DP150103522) to JDW and MAH. JDW is an NHMRC (Australia) Principal Research Fellow. Research at the FNI was also supported by the Victorian Government's Operational Infrastructure Support Program. WL acknowledges the University of Melbourne for an MIRS PhD award.