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Hydrophobic mismatch demonstrated for membranolytic peptides, and their use as molecular rulers to measure bilayer thickness in native cells

Grau-Campistany, A.; Strandberg, E.; Wadhwani, P.; Reichert, J.; Bürck, J.; Rabanal, F.; Ulrich, A.S.

Hydrophobic mismatch is a well-recognized principle in the interaction of transmembrane proteins with lipid bilayers. This concept was extended here to amphipathic membranolytic alpha-helices. Nine peptides with lengths between 14 and 28 amino acids were designed from repeated KIAGKIA motifs, and their helical nature was confirmed by circular dichroism spectroscopy. Biological assays for antimicrobial activity and hemolysis, as well as fluorescence vesicle leakage and solid-state NMR spectroscopy, were used to correlate peptide length with membranolytic activity. These data show that the formation of transmembrane pores is only possible under the condition of hydrophobic matching: the peptides have to be long enough to span the hydrophobic bilayer core to be able to induce vesicle leakage, kill bacteria, and cause hemolysis. By correlating the threshold lengths for biological activity with the biophysical results on model vesicles, the peptides could be utilized as molecular rulers to measure the membrane thickness in different cells.

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Volltext §
DOI: 10.5445/IR/1000046959
DOI: 10.1038/srep09388
Zitationen: 20
Web of Science
Zitationen: 20
Zugehörige Institution(en) am KIT Institut für Baugestaltung (Inst. f. Baugest.)
Institut für Biologische Grenzflächen (IBG)
Publikationstyp Zeitschriftenaufsatz
Jahr 2015
Sprache Englisch
Identifikator ISSN: 2045-2322
KITopen-ID: 1000046959
HGF-Programm 47.02.02 (POF III, LK 01)
Erschienen in Scientific Reports
Band 5
Seiten 9388/1-5
Bemerkung zur Veröffentlichung Gefördert durch den KIT-Publikationsfonds
Schlagworte Antibiotics; Peptides; Membrane biophysics; Membrane structure and assembly
Nachgewiesen in Scopus
Web of Science
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