| Literature DB >> 27052218 |
Jonathan Zerweck1, Erik Strandberg2, Jochen Bürck2, Johannes Reichert2, Parvesh Wadhwani2, Olga Kukharenko1, Anne S Ulrich3,4.
Abstract
PGLa and magainin 2 (MAG2) are amphiphilic α-helical frog peptides with synergistic antimicrobial activity. In vesicle leakage assays we observed the strongest synergy for equimolar mixtures of PGLa and MAG2. This result was consistent with solid-state (15)N-NMR data on the helix alignment in model membranes. The Hill coefficients determined from the vesicle leakage data showed that the heterodimeric (PGLa-MAG2) interactions were stronger than the homodimeric (PGLa-PGLa and MAG2-MAG2) interactions. This result was also reflected in the free energy of dimerization determined from oriented circular dichroism and quantitative solid-state (19)F-NMR analysis.Entities:
Keywords: Hill coefficients; Membrane-active amphiphilic helices; Peptide dimerization; Solid-state NMR; Synergistic antimicrobial peptides; Vesicle leakage assay
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Year: 2016 PMID： 27052218 DOI： 10.1007/s00249-016-1120-7
Source DB: PubMed Journal: Eur Biophys J ISSN： 0175-7571 Impact factor: 1.733