Reference : Synthetic model peptides for apolipoproteins. I. Design and properties of synthetic m...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/65872
Synthetic model peptides for apolipoproteins. I. Design and properties of synthetic model peptides for the amphipathic helices of the plasma apolipoproteins.
English
Brasseur, Robert mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Vanloo, B. [> > > >]
Deleys, R. [> > > >]
Lins, Laurence mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér. >]
Labeur, C. [> > > >]
Taveirne, J. [> > > >]
Ruysschaert, J. M. [> > > >]
Rosseneu, M. [> > > >]
1993
Biochimica et Biophysica Acta
1170
1
1-7
Yes (verified by ORBi)
International
0006-3002
[en] Amino Acid Sequence ; Apolipoproteins/chemical synthesis/chemistry ; Binding Sites ; Blood Proteins/chemistry ; Electrochemistry ; Humans ; Lipids/chemistry ; Models, Molecular ; Molecular Sequence Data ; Phospholipids/chemistry ; Stereoisomerism
[en] Amphipathic helical peptides are the lipid-binding motives of the plasma apolipoproteins, and synthetic peptide analogs have been used to unravel the mechanism of lipid association within this class of proteins. Hydrophobic interactions between the apolar amino acid residues belonging to the hydrophobic face of the amphipathic helices and the lipids are the major driving forces in the peptide-lipid association to form discoidal complexes. Ionic interactions and salt bridge formation between contiguous peptide chains in the complex can, however, contribute to the overall stability of the lipid-protein particle. This was studied by designing peptide analogs to the helical repeats of the apolipoproteins with variable degrees of salt bridge formation between adjacent peptide chains. The most stable conformation for pairs of synthetic peptides was calculated by energy minimisation together with the energy of interaction between peptides. The sequence of the peptides was derived from that of the 18A peptide synthesized by Segrest et al., and the theoretical calculations confirmed that ionic interactions between residues close to each other, along the edge of two adjacent anti-parallel peptides, can significantly contribute towards the stability of a peptide-phospholipid complex.
Researchers ; Professionals
http://hdl.handle.net/2268/65872

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Restricted access
5.pdfPublisher postprint1 MBRequest copy

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.