Lipid-destabilising properties of a peptide with structural plasticity
(2006) COST Meeting on Protein - Lipid Interactions — Location: Dubrovnik(Croatia) (6.October.2005)
Files
pdfdocument.pdf
Restricted Access - Adobe PDF
- 302.71 KB
Details
- Authors
- Abstract
- The Chameleon peptide (Chain) is a peptide designed from two regions of the GB1 protein, one folded as an a-helix and the other as a P structure. Depending on the environment, the Cham peptide adopts an a or a P 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 P structure in water and in a 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 Chant peptide (hydrophobicity, destabilising properties, conformation) to those of tilted peptides. The results suggest that Chant is a tilted peptide. Our study, together the presence of tilted fragments in transconformational proteins, suggests a relationship between tilted peptides and structural lability. (c) 2006 Elsevier Ireland Ltd. All rights reserved.
- Affiliations
Citations
Lorin, A., Thomas, A.-C., Stroobant, V., Brasseur, R., & Lins, L. (2006). Lipid-destabilising properties of a peptide with structural plasticity. Chemistry and Physics of Lipids, 141(1-2), 185-196. https://doi.org/10.1016/j.chemphyslip.2006.02.019 (Original work published 2006)