Replacement of the intervening amino acid sequence of a Syk-binding diphosphopeptide by a nonpeptide spacer with preservation of high affinity

Dekker, F.J., de Mol, N.J., van Ameijde, J., Fischer, M.J.E., Ruijtenbeek, R., Redegeld, F.A.M. and Liskamp, R.M.J. (2002) Replacement of the intervening amino acid sequence of a Syk-binding diphosphopeptide by a nonpeptide spacer with preservation of high affinity. ChemBioChem, 3(2-3), pp. 238-242. (doi:10.1002/1439-7633(20020301)3:2/3<238::AID-CBIC238>3.0.CO;2-W)

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Abstract

Divalent peptidomimetic compounds can bind a signal transduction protein and provide an avenue towards uncovering compounds capable of influencing or interfering with protein–protein interactions in general. High-affinity binding was realized by linking two relatively weakly interacting monophosphorylated peptides with an oligoethylene glycol spacer (see structure) the length of which was tuned by design.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Dekker, F.J., de Mol, N.J., van Ameijde, J., Fischer, M.J.E., Ruijtenbeek, R., Redegeld, F.A.M., and Liskamp, R.M.J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:ChemBioChem
ISSN:1439-4227
ISSN (Online):1439-7633

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