Cyclic phosphopeptides for interference with Grb2 SH2 domain signal transduction prepared by ring-closing metathesis and phosphorylation

Dekker, F.J., de Mol, N.J., Fischer, M.J.E., Kemmink, J. and Liskamp, R.M.J. (2003) Cyclic phosphopeptides for interference with Grb2 SH2 domain signal transduction prepared by ring-closing metathesis and phosphorylation. Organic and Biomolecular Chemistry, 1(19), pp. 3297-3303. (doi:10.1039/b306681a)

Full text not currently available from Enlighten.

Publisher's URL: http://dx.doi.org/10.1039/b306681a

Abstract

Cyclic phosphopeptides were prepared using ring-closing metathesis followed by phosphorylation. These cyclic phosphopeptides were designed to interact with the SH2 domain of Grb2, which is a signal transduction protein of importance as a target for antiproliferative drug development. Binding of these peptides to the Grb2 SH2 domain was evaluated by a surface plasmon resonance assay. High affinity binding to the Grb2 SH2 domain was maintained upon macrocyclization, thus indicating that this method can be used to assemble high affinity cyclic phosphopeptides that interfere with signal transduction cascades.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Dekker, F.J., de Mol, N.J., Fischer, M.J.E., Kemmink, J., and Liskamp, R.M.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Organic and Biomolecular Chemistry
ISSN:1477-0520
ISSN (Online):1477-0539

University Staff: Request a correction | Enlighten Editors: Update this record