The activity of the amphipathic peptide delta-lysin correlates with phospholipid acyl chain structure and bilayer elastic properties.

Biophysical Journal
Antje PokornyPaulo F F Almeida

Abstract

Release of lipid vesicle content induced by the amphipathic peptide delta-lysin was investigated as a function of lipid acyl chain length and degree of unsaturation for a series of phosphatidylcholines. Dye efflux and peptide binding were examined for three homologous lipid series: di-monounsaturated, di-polyunsaturated, and asymmetric phosphatidylcholines, with one saturated and one monounsaturated acyl chain. Except for the third series, peptide activity correlated with the first moment of the lateral pressure profile, which is a function of lipid acyl chain structure. In vesicles composed of asymmetric phosphatidylcholines, peptide binding and dye efflux are enhanced compared to symmetric, unsaturated lipids with similar pressure profiles. We attribute this to the entropically more favorable interaction of delta-lysin with partially saturated phospholipids. We find that lipid acyl chain structure has a major impact on the activity of delta-lysin and is likely to be an important factor contributing to the target specificity of amphipathic peptides.

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Citations

Jan 13, 2011·The Journal of Membrane Biology·William C Wimley, Kalina Hristova
Jul 15, 2009·Biochemistry·Lindsay E YandekPaulo F F Almeida
Oct 31, 2015·Biochimica Et Biophysica Acta·Natalie J MitchellAntje Pokorny
Jan 1, 2019·Australian Journal of Chemistry·William C Wimley, Kalina Hristova
Jan 19, 2021·Biophysical Journal·Sarah Y KimKalina Hristova
Jan 10, 2019·Chemical Reviews·Shantanu GuhaWilliam C Wimley

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