CHIPS binds to the phosphorylated N-terminus of the C5a-receptor

Bunschoten, A., Feitsma, L.J., Kruijtzer, J.A.W., de Haas, C.J.C., Liskamp, R.M.J. and Kemmink, J. (2010) CHIPS binds to the phosphorylated N-terminus of the C5a-receptor. Bioorganic and Medicinal Chemistry Letters, 20(11), pp. 3338-3340. (doi:10.1016/j.bmcl.2010.04.028)

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Abstract

Replacement of the sulfate groups, present in vivo on the N-terminus of the C5a-receptor (C5aR), by phosphate groups is explored. Phosphorylated mimics of the C5a-receptor N-terminus are synthesized and their binding to Chemotaxis Inhibitory Protein of Staphylococcus aureus (CHIPS) is studied by ITC and NMR. The phosphorylated C5aR mimics showed comparable binding affinity and a similar binding mode towards CHIPS compared to their sulfated forms. The activities of the phosphorylated peptides in a biological assay, however, were significantly lower compared to their sulfated counterparts.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Liskamp, Professor Robert
Authors: Bunschoten, A., Feitsma, L.J., Kruijtzer, J.A.W., de Haas, C.J.C., Liskamp, R.M.J., and Kemmink, J.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Bioorganic and Medicinal Chemistry Letters
ISSN:0960-894X
ISSN (Online):1464-3405

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