Reference : Tilted peptides: a structural motif involved in protein membrane insertion?
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/63327
Tilted peptides: a structural motif involved in protein membrane insertion?
English
Lins, Laurence mailto [Université de Liège - ULg > Chimie et bio-industries > biophysique moléc. numér. > >]
Brasseur, Robert mailto [Université de Liège - ULg > Chimie et bio-industries > Biophysique moléc. numér. >]
2008
Journal of Peptide Science : An Official Publication of the European Peptide Society
John Wiley & Sons, Inc
14
4
416-22
Yes (verified by ORBi)
International
1075-2617
Chichester
United Kingdom
[en] Adhesins, Bacterial/chemistry/genetics/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Bordetella pertussis/chemistry ; Hemagglutinins/chemistry/genetics/metabolism ; Hydrophobicity ; Lipid Bilayers/chemistry/metabolism ; Lipid Metabolism ; Lipids/chemistry ; Liposomes/chemistry ; Mass Spectrometry ; Membrane Proteins/metabolism ; Models, Molecular ; Molecular Sequence Data ; Peptide Fragments/chemistry/genetics/metabolism ; Peptides/chemical synthesis/chemistry ; Protein Binding ; Protein Structure, Secondary ; Spectroscopy, Fourier Transform Infrared
[en] Tilted peptides are short hydrophobic protein fragments characterized by an asymmetric distribution of their hydrophobic residues when helical. They are able to interact with a hydrophobic/hydrophilic interface (such as a lipid membrane) and to destabilize the organized system into which they insert. They were detected in viral fusion proteins and in proteins involved in different biological processes involving membrane insertion or translocation of the protein in which they are found. In this paper, we have analysed different protein domains related to membrane insertion with regard to their tilted properties. They are the N-terminal signal peptide of the filamentous haemagglutinin (FHA), a Bordetella pertussis protein secreted in high amount and the hydrophobic domain from proteins forming pores (i.e. ColIa, Bax and Bcl-2). From the predictions and the experimental approaches, we suggest that tilted peptides found in those proteins could have a more general role in the mechanism of insertion/translocation of proteins into/across membranes. For the signal sequences, they could help the protein machinery involved in protein secretion to be more active. In the case of toroidal pore formation, they could disturb the lipids, facilitating the insertion of the other more hydrophilic helices.
Researchers ; Professionals
http://hdl.handle.net/2268/63327
10.1002/psc.971
Lins Laurence et Brasseur Robert sont co-auteurs

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