Synthetic model peptides for apolipoproteins. I. Design and properties of synthetic model peptides for the amphipathic helices of the plasma apolipoproteins.
[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.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Brasseur, Robert ; Université de Liège - ULiège > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér.
Vanloo, B.
Deleys, R.
Lins, Laurence ; Université de Liège - ULiège > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie moléc. et numér.
Labeur, C.
Taveirne, J.
Ruysschaert, J. M.
Rosseneu, M.
Language :
English
Title :
Synthetic model peptides for apolipoproteins. I. Design and properties of synthetic model peptides for the amphipathic helices of the plasma apolipoproteins.
scite shows how a scientific paper has been cited by providing the context of the citation, a classification describing whether it supports, mentions, or contrasts the cited claim, and a label indicating in which section the citation was made.
Lins, Rosseneu, Ruysschaert, Brasseur Structure and function of apolipoproteins , M. Rosseneu, CRC Press, Boca Raton, FL; 1992, 261-268.
Rosseneu, Vanloo, Lins, De Pauw, Ruysschaert, Brasseur Structure and function of apolipoproteins , M. Rosseneu, CRC Press, Boca Raton, FL; 1992, 159-183.
Jonas Structure and function of apolipoproteins , M. Rosseneu, CRC Press, Boca Raton, FL; 1992, 217-254.
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