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Cited by 43Antimicrobial Peptides and ActivitiesLipid Membrane Structure and BehaviorAntimicrobial agents and applications

19F NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids

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Afonin, Sergii, Glaser, Ralf W., Sachse, Carsten, Salgado, Jesús, Wadhwani, Parvesh, Ulrich, Anne S.·2014·Biochimica et Biophysica Acta (BBA) - Biomembranes
DOI 10.1016/j.bbamem.2014.03.017
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Abstract

Many amphiphilic antimicrobial peptides permeabilize bacterial membranes via successive steps of binding, re-alignment and/or oligomerization. Here, we have systematically compared the lipid interactions of two structurally unrelated peptides: the cyclic β-pleated gramicidin S (GS), and the α-helical PGLa. (19)F NMR was used to screen their molecular alignment in various model membranes over a wide range of temperatures. Both peptides were found to respond to the phase state and composition of these different samples in a similar way. In phosphatidylcholines, both peptides first bind to the bilayer surface. Above a certain threshold concentration they can re-align and immerse more deeply into the hydrophobic core, which presumably involves oligomerization. Re-alignment is most favorable around the lipid chain melting temperature, and also promoted by decreasing bilayer thickness. The presence of anionic lipids has no influence in fluid membranes, but in the gel phase the alignment states are more complex. Unsaturated acyl chains and other lipids with intrinsic negative curvature prevent re-alignment, hence GS and PGLa do not insert into mixtures resembling bacterial membranes, nor into bacterial lipid extracts. Cholesterol, which is present in high concentrations in animal membranes, even leads to an expulsion of the peptides from the bilayer and prevents their binding altogether. However, a very low cholesterol content of 10% was found to promote binding and re-alignment of both peptides. Overall, these findings show that the ability of amphiphilic peptides to re-align and immerse into a membrane is determined by the physico-chemical properties of the lipids, such as spontaneous curvature. This idea is reinforced by the remarkably similar behavior observed here for two structurally unrelated molecules (with different conformation, size, shape, charge), which further suggests that their activity at the membrane level is largely governed by the properties of the constituent lipids, while the selectivity towards different cell types is additionally ruled by electrostatic attraction between peptide and cell surface. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.

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Authors
Afonin, S., Glaser, R. W., Sachse, C., Salgado, J., Wadhwani, P., & Ulrich, A. S.
Affiliations
  • Karlsruhe Institute of Technology (DE)
  • Friedrich Schiller University Jena (DE)
  • European Molecular Biology Laboratory (DE)
  • Universitat de València (ES)
Corresponding author
Ulrich, Anne S.
ORCID
Venue
Biochimica et Biophysica Acta (BBA) - Biomembranes
Publisher
Elsevier BV
Published
2014-09
Volume
1838
Issue
9
Pages
2260-2268
ISSN
0005-2736 (ISSN-L)
DOI
10.1016/j.bbamem.2014.03.017
OpenAlex
W2007391269
Cited by
43
References
80
Citations by year
2026: 2 · 2024: 1 · 2023: 1 · 2022: 3 · 2020: 5 · 2019: 2 · 2018: 5 · 2017: 7 · 2016: 6 · 2015: 8 · 2014: 3
FWCI
6.07
Type
journal article
Language
en
Open access
Licence
Locations
  • Biochimica et Biophysica Acta (BBA) - Biomembranes (publishedVersion)
  • PubMed (publishedVersion)
  • JuSER (Forschungszentrum Jülich) (submittedVersion)
Funders
Spanish MINECO (BFU2010-19118)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Lipid Membrane Structure and Behavior
  • Physical Sciences › Chemistry › Organic Chemistry › Antimicrobial agents and applications
Keywords
antimicrobial peptides, gramicidin S, PGLa, peptide-lipid interactions, membrane permeabilization, peptide oligomerization, spontaneous curvature, bilayer thickness, cholesterol, anionic lipids, unsaturated acyl chains, gel phase, phosphatidylcholine, model membranes, 19F NMR
MeSH terms
Amino Acid Sequence, Bacteria, Cell Membrane, Gramicidin, Humans, Lipid Bilayers, Membrane Lipids, Protein Precursors, Protein Structure, Secondary, Nuclear Magnetic Resonance, Biomolecular

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