Literature DB >> 10824736

Tilted peptides: a motif for membrane destabilization (hypothesis).

R Brasseur1.   

Abstract

Cell life depends on the dynamics of molecular processes: molecule folding, organelle building and transformations involving membrane fusion, protein activation and degradation. To carry out these processes, the hydrophilic/hydrophobic interfaces of amphipathic systems such as membranes and native proteins must be disrupted. In the past decade, protein fragments acting in the disruption of interfaces have been evidenced: they are named the tilted or oblique peptides. Due to a peculiar distribution of hydrophobicity, they can disrupt hydrophobicity interfaces. Tilted peptides should be present in many proteins involved in various stages of cell life. This hypothesis overviews their discovery, describes how they are detected and discusses how they could be involved in dynamic biological processes.

Entities:  

Mesh:

Substances:

Year:  2000        PMID: 10824736     DOI: 10.1080/096876800294461

Source DB:  PubMed          Journal:  Mol Membr Biol        ISSN: 0968-7688            Impact factor:   2.857


  12 in total

1.  Statistical thermodynamics of membrane bending-mediated protein-protein attractions.

Authors:  T Chou; K S Kim; G Oster
Journal:  Biophys J       Date:  2001-03       Impact factor: 4.033

2.  A theoretical investigation into the lipid interactions of m-calpain.

Authors:  A Daman; F Harris; S Biswas; J Wallace; D A Phoenix
Journal:  Mol Cell Biochem       Date:  2001-07       Impact factor: 3.396

3.  Distribution of hydrophobic residues is crucial for the fusogenic properties of the Ebola virus GP2 fusion peptide.

Authors:  B Adam; L Lins; V Stroobant; A Thomas; R Brasseur
Journal:  J Virol       Date:  2004-02       Impact factor: 5.103

4.  Prolactin/growth hormone-derived antiangiogenic peptides highlight a potential role of tilted peptides in angiogenesis.

Authors:  Ngoc-Quynh-Nhu Nguyen; Sebastien P Tabruyn; Laurence Lins; Michelle Lion; Anne M Cornet; Florence Lair; Francoise Rentier-Delrue; Robert Brasseur; Joseph A Martial; Ingrid Struman
Journal:  Proc Natl Acad Sci U S A       Date:  2006-09-14       Impact factor: 11.205

5.  Secondary structure and distribution of fusogenic LV-peptides in lipid membranes.

Authors:  J Ollesch; B C Poschner; J Nikolaus; M W Hofmann; A Herrmann; K Gerwert; D Langosch
Journal:  Eur Biophys J       Date:  2007-11-24       Impact factor: 1.733

6.  "De novo" design of peptides with specific lipid-binding properties.

Authors:  L Lins; B Charloteaux; C Heinen; A Thomas; R Brasseur
Journal:  Biophys J       Date:  2005-11-04       Impact factor: 4.033

7.  Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins.

Authors:  Maddalena Venturoli; Berend Smit; Maria Maddalena Sperotto
Journal:  Biophys J       Date:  2005-03       Impact factor: 4.033

Review 8.  Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapy.

Authors:  Himanshu Garg; Mathias Viard; Amy Jacobs; Robert Blumenthal
Journal:  Curr Top Med Chem       Date:  2011-12       Impact factor: 3.295

9.  Investigations into the ability of the peptide, HAL18, to interact with bacterial membranes.

Authors:  Sarah R Dennison; Young Soo Kim; Hyung Joon Cha; David A Phoenix
Journal:  Eur Biophys J       Date:  2008-07-04       Impact factor: 1.733

10.  Common molecular mechanism of amyloid pore formation by Alzheimer's β-amyloid peptide and α-synuclein.

Authors:  Coralie Di Scala; Nouara Yahi; Sonia Boutemeur; Alessandra Flores; Léa Rodriguez; Henri Chahinian; Jacques Fantini
Journal:  Sci Rep       Date:  2016-06-29       Impact factor: 4.379

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.