Abstract：
:The conformational change of the model peptide Ac-K-G-R-G-D-G-amide induced by a phospholipidic interface was investigated by proton nuclear magnetic resonance (1H NMR). In aqueous solution, the free peptide is highly flexible and disordered, even in the presence of deuterated dodecyl-phosphocholine (DPC-d38) micelles which mimic a membrane interface. The lipopeptide, obtained by grafting a lipid anchor [2,3-dipalmitoyl-D-(+)-glyceric acid] to the lysine side chain of the peptide, was studied by standard 2D 1H NMR spectroscopy combined with distance geometry and simulated annealing calculations. When anchored to a micelle interface, the peptide acquires a definite turn (II/I') conformation. We were also able to describe precisely the conformation of the diacylglyceric fragment of the lipopeptide in a lipid environment and to establish the average orientation of the peptide segment with respect to the micelle surface.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Macquaire F,Baleux F,Giaccobi E,Huynh-Dinh T,Neumann JM,Sanson Adoi
10.1021/bi00124a018subject
Has Abstractpub_date
1992-03-10 00:00:00pages
2576-82issue
9eissn
0006-2960issn
1520-4995journal_volume
31pub_type
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