Structure–activity relationships of the antimicrobial peptide gramicidin S and its analogs: Aqueous solubility, self-association, conformation, antimicrobial activity and interaction with model lipid membranes

Author:

Abraham Thomas,Prenner Elmar J.,Lewis Ruthven N.A.H.,Mant Colin T.,Keller Sandro,Hodges Robert S.,McElhaney Ronald N.

Funder

Canadian Institutes of Health Research (R.N.M.)

Alberta Heritage Foundation for Medical Research (R.N.M.)

National Institutes of Health (R.S.H.)

John Stewart Chair in Peptide Chemistry (R.S.H.)

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference51 articles.

1. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes;Prenner;Biochim. Biophys. Acta,1999

2. Antimicrobial peptides in innate immunity;Ganz,2001

3. The commercial development of the antimicrobial peptide Pexiganan;Zasloff,2001

4. Origins and evolution of antibiotic and multiple antibiotic resistance in bacteria;Hall,2001

5. Are we on the threshold of the post-antibiotics era?;Lohner,2001

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