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 |
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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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