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Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes

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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 15N-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 19F-NMR analysis.

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Acknowledgments

This work was supported financially by the Center for Functional Nanotechnology (CFN) (E1.2). We thank Andrea Eisele, Kerstin Scheubeck and Markus Schmitt for technical support.

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Authors and Affiliations

  1. Karlsruhe Institute of Technology (KIT), Institute of Organic Chemistry, Fritz-Haber-Weg 6, 76131, Karlsruhe, Germany

    Jonathan Zerweck, Olga Kukharenko & Anne S. Ulrich

  2. KIT, Institute of Biological Interfaces (IBG-2), POB 3640, 76021, Karlsruhe, Germany

    Erik Strandberg, Jochen Bürck, Johannes Reichert, Parvesh Wadhwani & Anne S. Ulrich

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  1. Jonathan Zerweck
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  2. Erik Strandberg
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Zerweck, J., Strandberg, E., Bürck, J. et al. Homo- and heteromeric interaction strengths of the synergistic antimicrobial peptides PGLa and magainin 2 in membranes. Eur Biophys J 45, 535–547 (2016). https://doi.org/10.1007/s00249-016-1120-7

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