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Membrane Thinning and Thickening Induced by Membrane-Active Amphipathic Peptides

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

Abstract (englisch):
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 2H-NMR and grazing incidence small angle X-ray scattering (GISAXS) on oriented phospholipid bilayers we ... mehr

Zugehörige Institution(en) am KIT Institut für Biologische Grenzflächen (IBG)
Institut für Beschleunigerphysik und Technologie (IBPT)
Institut für Organische Chemie (IOC)
Publikationstyp Zeitschriftenaufsatz
Jahr 2016
Sprache Englisch
Identifikator DOI: 10.3389/fcell.2016.00065
ISSN: 2296-634X
URN: urn:nbn:de:swb:90-578253
KITopen ID: 1000057825
HGF-Programm 47.02.02; LK 01
Erschienen in Frontiers in cell and developmental biology
Band 4
Seiten 65
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