Hydrophobic Mismatch Demonstrated for Membranolytic Peptides, and Their Use As Molecular Rulers to Measure Bilayer Thickness in Native Cells

Overview

Journal Sci Rep

Specialty Science

Date 2015 Mar 26

PMID 25807192

Citations 22

Authors

Ariadna Grau-Campistany

Erik Strandberg

Parvesh Wadhwani

Johannes Reichert

Jochen Burck

Francesc Rabanal

Anne S Ulrich

Affiliations

Soon will be listed here.

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.

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