Structural studies of two antiaggregant RGDW peptides by lH and 13C NMR

BRUNO KIEFFER, GEORGES MER, ANDRÉ MANN, JEAN‐FRANÇOIS ‐F LEFÈVRE

Research output: Contribution to journalArticle

17 Scopus citations

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 languageEnglish (US)
Pages (from-to)70-79
Number of pages10
JournalInternational Journal of Peptide and Protein Research
Volume44
Issue number1
DOIs
StatePublished - Jul 1994

Keywords

  • NMR
  • RGD peptide
  • cell adhesion

ASJC Scopus subject areas

  • Biochemistry

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