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)

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 <i>Staphylococcus aureus</i> (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