Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/108766
Title: Extending the hydrophobic mismatch concept to amphiphilic membranolytic peptides
Author: Grau Campistany, Ariadna
Strandberg, Erik
Wadhwani, Parvesh
Rabanal Anglada, Francesc
Ullrich, Anne S.
Keywords: Pèptids
Membranes (Biologia)
Bicapes lipídiques
Biofísica
Peptides
Membranes (Biology)
Lipid bilayers
Biophysics
Issue Date: 10-Mar-2016
Publisher: American Chemical Society
Abstract: A series of nine amphiphilic, pore-forming α-helical KIA peptides (KIAGKIA repeats) with lengths between 14 and 28 residues were studied by solidstate 15N NMR to determine their alignment in oriented lipid bilayers. In a 2:1 mixture of 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) with its corresponding 1- myristoyl-2-hydroxy-sn-glycero-3-phosphocholine (lyso-MPC), which has a highly positive spontaneous curvature, the helix tilt angle was found to vary steadily with peptide length. The shortest peptide was aligned transmembrane and upright, while the longer ones successively became tilted away from the membrane normal. This behavior is in agreement with the hydrophobic matching concept, conceived so far only for hydrophobic helices. In 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine, with a negative spontaneous curvature, all KIA peptides remained flat on the bilayer surface, while the cylindrical DMPC lipids permitted a slight tilt. Peptide insertion thus depends critically on the intrinsic lipid curvature, and helix orientation is then fine-tuned by membrane thickness. A refined toroidal pore model is proposed.
Note: Versió postprint del document publicat a: https://doi.org/10.1021/acs.jpclett.6b00136
It is part of: Journal of Physical Chemistry Letters, 2016, vol. 7, num. 7, p. 1116-1120
Related resource: https://doi.org/10.1021/acs.jpclett.6b00136
URI: http://hdl.handle.net/2445/108766
ISSN: 1948-7185
Appears in Collections:Articles publicats en revistes (Química Inorgànica i Orgànica)

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