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.
Original language | English (US) |
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Pages (from-to) | 70-79 |
Number of pages | 10 |
Journal | International Journal of Peptide and Protein Research |
Volume | 44 |
Issue number | 1 |
DOIs | |
State | Published - Jul 1994 |
Keywords
- NMR
- RGD peptide
- cell adhesion
ASJC Scopus subject areas
- Biochemistry