Literature DB >> 18535783

A dynamic view of peptides and proteins in membranes.

B Bechinger1.   

Abstract

Biological membranes are highly dynamic supramolecular arrangements of lipids and proteins, which fulfill key cellular functions. Relatively few high-resolution membrane protein structures are known to date, although during recent years the structural databases have expanded at an accelerated pace. In some instances the structures of reaction intermediates provide a stroboscopic view on the conformational changes involved in protein function. Other biophysical approaches add dynamic aspects and allow one to investigate the interactions with the lipid bilayers. Membrane-active peptides fulfill many important functions in nature as they act as antimicrobials, channels, transporters or hormones, and their studies have much increased our understanding of polypeptide-membrane interactions. Interestingly several proteins have been identified that interact with the membrane as loose arrays of domains. Such conformations easily escape classical high-resolution structural analysis and the lessons learned from peptides may therefore be instructive for our understanding of the functioning of such membrane proteins.

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Year:  2008        PMID: 18535783     DOI: 10.1007/s00018-008-8125-z

Source DB:  PubMed          Journal:  Cell Mol Life Sci        ISSN: 1420-682X            Impact factor:   9.261


  11 in total

Review 1.  Single-spanning transmembrane domains in cell growth and cell-cell interactions: More than meets the eye?

Authors:  Pierre Hubert; Paul Sawma; Jean-Pierre Duneau; Jonathan Khao; Jérôme Hénin; Dominique Bagnard; James Sturgis
Journal:  Cell Adh Migr       Date:  2010-04-20       Impact factor: 3.405

Review 2.  Toward understanding protocell mechanosensation.

Authors:  Daniel Balleza
Journal:  Orig Life Evol Biosph       Date:  2010-11-17       Impact factor: 1.950

3.  Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.

Authors:  Jarbas M Resende; Cléria Mendonça Moraes; Victor H O Munhoz; Christopher Aisenbrey; Rodrigo M Verly; Philippe Bertani; Amary Cesar; Dorila Piló-Veloso; Burkhard Bechinger
Journal:  Proc Natl Acad Sci U S A       Date:  2009-09-14       Impact factor: 11.205

4.  Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formers.

Authors:  Aram J Krauson; Jing He; William C Wimley
Journal:  Biochim Biophys Acta       Date:  2012-07

5.  Adsorption of proteins on a lipid bilayer.

Authors:  Vladimir P Zhdanov; Bengt Kasemo
Journal:  Eur Biophys J       Date:  2010-04-13       Impact factor: 1.733

6.  Reversible liposome association induced by LAH4: a peptide with potent antimicrobial and nucleic acid transfection activities.

Authors:  Arnaud Marquette; Bernard Lorber; Burkhard Bechinger
Journal:  Biophys J       Date:  2010-06-02       Impact factor: 4.033

7.  NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action, and DNA transfection.

Authors:  Julia Georgescu; Victor H O Munhoz; Burkhard Bechinger
Journal:  Biophys J       Date:  2010-10-20       Impact factor: 4.033

Review 8.  Life at the border: adaptation of proteins to anisotropic membrane environment.

Authors:  Irina D Pogozheva; Henry I Mosberg; Andrei L Lomize
Journal:  Protein Sci       Date:  2014-07-02       Impact factor: 6.725

9.  Antifungal activities of peptides derived from domain 5 of high-molecular-weight kininogen.

Authors:  Andreas Sonesson; Emma Andersson Nordahl; Martin Malmsten; Artur Schmidtchen
Journal:  Int J Pept       Date:  2011-09-14

Review 10.  Mechanistic Landscape of Membrane-Permeabilizing Peptides.

Authors:  Shantanu Guha; Jenisha Ghimire; Eric Wu; William C Wimley
Journal:  Chem Rev       Date:  2019-01-09       Impact factor: 72.087

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