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. 2010 Nov 26;30(1):5–16. doi: 10.1038/emboj.2010.299

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Copyright © 2011, European Molecular Biology Organization

This is an open-access article distributed under the terms of the Creative Commons Attribution Noncommercial No Derivative Works 3.0 Unported License, which permits distribution and reproduction in any medium, provided the original author and source are credited. This license does not permit commercial exploitation or the creation of derivative works without specific permission.

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The membrane remodelling activity of different Pex11-Amph peptides. (A) Superimposition of a 3D model of ideal α-helices of Pex11-Amph (red) and the e-Pex11-Amph mutant (green) with marked mutations. The mutant peptide e-Pex11-Amph contains bulkier tryptophane residues on the hydrophobic interface of the amphipathic helix. (B) Electron micrographs of SUVs of a phospholipid content resembling peroxisomal membranes following incubation with the e-Pex11-Amph peptide. Besides typical tubules observed for Pex11-Amph, low diameter tubules could often be observed (black arrow). (C) The e-Pex11-Amph peptide also induces formation of multiple low diameter tubules developing from single liposomes (black arrows). (D) Helical wheel representation of the region comprising the Pex11-Amph from S. cerevisiae (residues 58–75 of S.c.Pex11) showing the hydrophobic (yellow) and polar, positively charged (blue) interfaces of the helix. (E) Electron micrographs of PC/PE/PS/PI/CL SUVs following incubation with Sc-Pex11-Amph peptide showing extensive tubulation of liposomes. (F) Helical wheel representation of the Pex11-Amph from H. polymorpha (residues 62–79 of Hp-Pex11) revealing the amphipathic properties of the α-helix with a charged polar surface similar to the Pex11-Amph motifs from P. chrysogenum and S. cerevisiae. (G) Incubation of Hp-Pex11-Amph with liposomes with phospholipid content resembling that of the peroxisomal membrane causes efficient tubulation of vesicles. (H) Representation of Pex11-Amph from H. sapiens (residues 58–75 of Hs-Pex11α) in the helical wheel mode shows the amphipathic properties of this motif. In contrast to fungal Pex11-Amph, the corresponding motif in human Pex11α contains a polar interface that is less enriched in basic amino acids. (I) Electron micrograph of PC/PE/PS/PI/CL liposomes after addition of the Hs-Pex11-Amph peptide showing that the amphipathic helix of human Pex11α is active in vesicle tubulation. The observed tubules were usually shorter than for other Pex11-Amph peptides. Scale bars represent 100 nm.