Structural studies of two antiaggregant RGDW peptides by lH and 13C NMR
- 1 July 1994
- journal article
- Published by Wiley in International Journal of Peptide and Protein Research
- Vol. 44 (1) , 70-79
- https://doi.org/10.1111/j.1399-3011.1994.tb00406.x
Abstract
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′β-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.Keywords
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