ISSN:
1573-3904
Keywords:
lactam bridge peptides
;
tyrosine kinases
;
tyrosine phosphorylation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The heptapeptide EDNEYTA, which reproduces the main autophosphorylation site of Src, has been previously shown to be a good substrate for both Src and Syk tyrosine kinases [Ruzza, P., et al., J. Pept. Sci., 2 (1996) 325]. Four lactam bridge conformationally constrained analogues of this peptide were synthesized by classical solution methods and screened for their suitability as c-Fgr and Syk tyrosine kinase substrates. The kinetic data obtained indicate that the different rings of the lactam peptides influence the capability of the peptides to act as PTK substrates. In general cyclization decreases the peptide phosphorylability, however the sequence containing the greatest lactam ring, ED(EEYTK), resulted in an especially suitable and selective substrate for Syk tyrosine kinase.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1008824024570
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