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Synthesis and characterization of photoactivatable peptide agonists of the human thrombin receptor.

Abstract
Chemical synthesis and biochemical analysis of modified agonist peptides of the human thrombin receptor derived from the sequence SFLLRNP containing photoactivatable azido groups and biotin for sensitive detection is described. Substitution of leucine in position three with p-azidophenylalanine and extension of the C-terminus with a KGGK spacer containing biotin covalently linked to the side chain of the C-terminal lysine residue resulted in an active receptor agonist as determined by intracellular Ca2+ mobilization in human erythroleukemia (HEL) cells. In contrast, substitution of phenylalanine in position two with p-azidophenylalanine reduced agonist activity significantly.
AuthorsR Bischoff, Y Cordier, U B Rasmussen, Y Schlesinger, C Gachet, M Jaquinod, B Tripet, P C Chong, A Pavirani
JournalFEBS letters (FEBS Lett) Vol. 349 Issue 2 Pg. 301-6 (Aug 01 1994) ISSN: 0014-5793 [Print] England
PMID8050586 (Publication Type: Journal Article)
Chemical References
  • Peptides
  • Receptors, Thrombin
Topics
  • Amino Acid Sequence
  • Humans
  • Leukemia, Erythroblastic, Acute
  • Molecular Sequence Data
  • Peptides (metabolism)
  • Photochemistry
  • Receptors, Thrombin (metabolism)
  • Tumor Cells, Cultured

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