Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/67368
Title: Hydrophobic mismatch demonstrated for membranolytic peptides and their use as molecular rulers to measure bilayer thickness in native cells
Author: Grau Campistany, Ariadna
Strandberg, Erik
Wadhwani, Parvesh
Reichert, Johannes
Bürck, Jochen
Rabanal Anglada, Francesc
Ullrich, Anne S.
Keywords: Antibiòtics
Pèptids
Membranes (Biologia)
Biofísica
Antibiotics
Peptides
Membranes (Biology)
Biophysics
Issue Date: 25-Mar-2015
Publisher: Nature Publishing Group
Abstract: Hydrophobic mismatch is a well-recognized principle in the interaction of transmembrane proteins with lipid bilayers. This concept was extended here to amphipathic membranolytic α-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.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1038/srep09388
It is part of: Scientific Reports, 2015, vol. 5, num. 9388, p. 1-9
Related resource: http://dx.doi.org/10.1038/srep09388
URI: http://hdl.handle.net/2445/67368
ISSN: 2045-2322
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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