Structural studies of two antiaggregant RGDW peptides by 1H and 13C NMR.
The structural features of Arg-Gly-Asp-related sequences have been investigated by 1H and 13C NMR. Two linear peptides which inhibit platelet aggregation with a high efficiency have been studied: D-Arg-Gly-Asp-Trp and L-Arg-Gly-Asp-Trp. Analysis of pH titration effects, amide proton exchange rates and inter-proton distances obtained from ROESY spectra suggest that these small fragments predominantly adopt a type II' beta-turn structure in solution. Folding features of a non-active cyclic peptide based on the same sequence (cyclo-[Arg-Gly-Asp-Trp]2) have also been investigated. The biological relevance of these structures is discussed.
CNRS-UPR 9003, ESBS, Strasbourg, France.
B
B
Kieffer
G
G
Mer
A
A
Mann
J F
JF
Lefèvre
D000595:Amino Acid Sequence; D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry; D010975:Platelet Aggregation Inhibitors / Q000737:chemistry*; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D010455:Peptides; D010975:Platelet Aggregation Inhibitors; C047981:arginyl-glycyl-aspartic acid