Lipid-Destabilising Properties Of A Peptide With Structural Plasticity

[en] The Chameleon peptide (Cham) is a peptide designed from two regions of the GB1 protein, one folded as an alpha-helix and the other as a beta structure. Depending on the environment, the Cham peptide adopts an alpha or a beta conformation when inserted in different locations of GB1. This environment dependence is also observed for tilted peptides. These short protein fragments, able to destabilise organised system, are mainly folded in beta structure in water and in alpha helix in a hydrophobic environment, like the lipid bilayer. In this paper, we tested whether the Cham peptide can be qualified as a tilted peptide. For this, we have compared the properties of Cham peptide (hydrophobicity, destabilising properties, conformation) to those of tilted peptides. The results suggest that Cham is a tilted peptide. Our study, together the presence of tilted fragments in transconformational proteins, suggests a relationship between tilted peptides and structural lability.

Disciplines :

Biochemistry, biophysics & molecular biology

Author, co-author :

Lorin, A.

Thomas, Annick ; Université de Liège - ULiège > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér.

Stroobant, V.

Brasseur, Robert ; Université de Liège - ULiège > Gembloux Agro-Bio Tech

Lins, Laurence ; Université de Liège - ULiège > Gembloux Agro-Bio Tech

Language :

English

Title :

Lipid-Destabilising Properties Of A Peptide With Structural Plasticity

Publication date :

2006

Journal title :

Chemistry and Physics of Lipids

ISSN :

0009-3084

Publisher :

Elsevier, Netherlands

Volume :

141

Issue :

1-2

Pages :

185-196
185-96

Peer reviewed :

Peer Reviewed verified by ORBi

Available on ORBi :

since 23 June 2010

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