CHIPS binds to the phosphorylated N-terminus of the C5a-receptor.
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.
Bunschoten
Anton
A
Medicinal Chemistry & Chemical Biology, Faculty of Science, Utrecht University, Sorbonnelaan 16, 3584 CA, Utrecht, The Netherlands.
Feitsma
Louris J
LJ
Kruijtzer
John A W
JA
de Haas
Carla J C
CJ
Liskamp
Rob M J
RM
Kemmink
Johan
J
D001426:Bacterial Proteins / Q000378:metabolism*; D018716:Molecular Mimicry; D010766:Phosphorylation; D011485:Protein Binding; D044087:Receptor, Anaphylatoxin C5a / Q000378:metabolism*
D001426:Bacterial Proteins; D044087:Receptor, Anaphylatoxin C5a; C493134:chemotaxis inhibitory protein, Staphylococcus aureus