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Grage SL, Afonin S, Kara S, et al. Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides. Front Cell Dev Biol. 2016;4:65doi: 10.3389/fcell.2016.00065.
Grage, S. L., Afonin, S., Kara, S., Buth, G., & Ulrich, A. S. (2016). Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides. Frontiers in cell and developmental biology, 465. https://doi.org/10.3389/fcell.2016.00065
Grage, Stephan L, et al. "Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides." Frontiers in cell and developmental biology vol. 4 (2016): 65. doi: https://doi.org/10.3389/fcell.2016.00065
Grage SL, Afonin S, Kara S, Buth G, Ulrich AS. Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides. Front Cell Dev Biol. 2016 Jun 24;4:65. doi: 10.3389/fcell.2016.00065. eCollection 2016. PMID: 27595096; PMCID: PMC4999517.
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Front Cell Dev Biol. 2016 Jun 24;4:65. doi: 10.3389/fcell.2016.00065. eCollection 2016.

Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides.

Frontiers in cell and developmental biology

Stephan L Grage, Sergii Afonin, Sezgin Kara, Gernot Buth, Anne S Ulrich

Affiliations

  1. Karlsruhe Institute of Technology, Institute of Biological Interfaces Karlsruhe, Germany.
  2. Karlsruhe Institute of Technology, Institute of Organic Chemistry Karlsruhe, Germany.
  3. Karlsruhe Institute of Technology, Institute for Accelerator Physics and Technology Karlsruhe, Germany.
  4. Karlsruhe Institute of Technology, Institute of Biological InterfacesKarlsruhe, Germany; Karlsruhe Institute of Technology, Institute of Organic ChemistryKarlsruhe, Germany.

PMID: 27595096 PMCID: PMC4999517 DOI: 10.3389/fcell.2016.00065

Abstract

Membrane thinning has been discussed as a fundamental mechanism by which antimicrobial peptides can perturb cellular membranes. To understand which factors play a role in this process, we compared several amphipathic peptides with different structures, sizes and functions in their influence on the lipid bilayer thickness. PGLa and magainin 2 from X. laevis were studied as typical representatives of antimicrobial cationic amphipathic α-helices. A 1:1 mixture of these peptides, which is known to possess synergistically enhanced activity, allowed us to evaluate whether and how this synergistic interaction correlates with changes in membrane thickness. Other systems investigated here include the α-helical stress-response peptide TisB from E. coli (which forms membrane-spanning dimers), as well as gramicidin S from A. migulanus (a natural antibiotic), and BP100 (designer-made antimicrobial and cell penetrating peptide). The latter two are very short, with a circular β-pleated and a compact α-helical structure, respectively. Solid-state (2)H-NMR and grazing incidence small angle X-ray scattering (GISAXS) on oriented phospholipid bilayers were used as complementary techniques to access the hydrophobic thickness as well as the bilayer-bilayer repeat distance including the water layer in between. This way, we found that magainin 2, gramicidin S, and BP100 induced membrane thinning, as expected for amphiphilic peptides residing in the polar/apolar interface of the bilayer. PGLa, on the other hand, decreased the hydrophobic thickness only at very high peptide:lipid ratios, and did not change the bilayer-bilayer repeat distance. TisB even caused an increase in the hydrophobic thickness and repeat distance. When reconstituted as a mixture, PGLa and magainin 2 showed a moderate thinning effect which was less than that of magainin 2 alone, hence their synergistically enhanced activity does not seem to correlate with a modulation of membrane thickness. Overall, the absence of a typical thinning response in the case of PGLa, and the increase in the repeat distance and membrane thickening observed for TisB, demonstrate that the concept of peptide-induced membrane thinning cannot be generalized. Instead, these results suggest that different factors contribute to the resulting changes in membrane thickness, such as the peptide orientation in the bilayer, and/or bilayer adaptation to hydrophobic mismatch.

Keywords: antimicrobial and cell penetrating peptides; gramicidin S; grazing incidence small angle X-ray scattering; lipid bilayer thickness; magainin; membrane thinning; oriented bilayer samples; solid-state deuterium nuclear magnetic resonance

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