Literature DB >> 11241210

Modulation of membrane curvature by peptides.

R M Epand1, R F Epand.   

Abstract

The fusion of two stable bilayers likely proceeds through intermediates in which the membrane acquires curvature. The insertion of peptides into the membrane will affect its curvature tendency. Studies with a number of small viral fusion peptides indicate that these peptides promote negative curvature at low concentration. This is in accord with the curvature requirements to initiate membrane fusion according to the stalk-pore model. Although a characteristic of fusion peptides, the promotion of negative curvature is only one of several mechanisms by which fusion proteins accelerate the rate of fusion. In addition, the fusion peptide itself, as well as other regions in the viral fusion protein, facilitates membrane fusion by mechanisms that are largely independent of curvature. Leakage of the internal aqueous contents of liposomes is another manifestation of the alteration of membrane properties. Peptides exhibit quite different relative potencies between fusion and leakage that is determined by the structure and mode of insertion of the peptide into the membrane.

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Year:  2000        PMID: 11241210     DOI: 10.1002/1097-0282(2000)55:5<358::AID-BIP1009>3.0.CO;2-8

Source DB:  PubMed          Journal:  Biopolymers        ISSN: 0006-3525            Impact factor:   2.505


  14 in total

1.  Conformational partitioning of the fusion peptide of HIV-1 gp41 and its structural analogs in bilayer membranes.

Authors:  Michael W Maddox; Marjorie L Longo
Journal:  Biophys J       Date:  2002-12       Impact factor: 4.033

2.  Hydrophobic surfactant proteins strongly induce negative curvature.

Authors:  Mariya Chavarha; Ryan W Loney; Shankar B Rananavare; Stephen B Hall
Journal:  Biophys J       Date:  2015-07-07       Impact factor: 4.033

3.  HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.

Authors:  Alex L Lai; Jack H Freed
Journal:  Biophys J       Date:  2014-01-07       Impact factor: 4.033

4.  N-terminal α-helix-independent membrane interactions facilitate adenovirus protein VI induction of membrane tubule formation.

Authors:  Oana Maier; Christopher M Wiethoff
Journal:  Virology       Date:  2010-09-25       Impact factor: 3.616

5.  HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics.

Authors:  Stephanie Tristram-Nagle; Rob Chan; Edgar Kooijman; Pradeep Uppamoochikkal; Wei Qiang; David P Weliky; John F Nagle
Journal:  J Mol Biol       Date:  2010-07-22       Impact factor: 5.469

Review 6.  The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.

Authors:  Justin L Lorieau; John M Louis; Ad Bax
Journal:  Biopolymers       Date:  2012-09-26       Impact factor: 2.505

Review 7.  Adenovirus membrane penetration: Tickling the tail of a sleeping dragon.

Authors:  Christopher M Wiethoff; Glen R Nemerow
Journal:  Virology       Date:  2015-03-19       Impact factor: 3.616

8.  An N-terminal domain of adenovirus protein VI fragments membranes by inducing positive membrane curvature.

Authors:  Oana Maier; Debra L Galan; Harald Wodrich; Christopher M Wiethoff
Journal:  Virology       Date:  2010-04-20       Impact factor: 3.616

9.  Effect of the HIV-1 fusion peptide on the mechanical properties and leaflet coupling of lipid bilayers.

Authors:  P Shchelokovskyy; S Tristram-Nagle; R Dimova
Journal:  New J Phys       Date:  2011-02       Impact factor: 3.729

10.  Architecture of a nascent viral fusion pore.

Authors:  Kelly K Lee
Journal:  EMBO J       Date:  2010-02-18       Impact factor: 11.598

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