Medicinal Chemistry & Chemical Biology, Faculty of Science, Utrecht University, Sorbonnelaan 16, 3584 CA, Utrecht, The Netherlands.
Bioorg Med Chem Lett. 2010 Jun 1;20(11):3338-40. doi: 10.1016/j.bmcl.2010.04.028. Epub 2010 Apr 14.
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.
探索体内存在于 C5a 受体（C5aR）N 端的硫酸根基团被磷酸基团取代的情况。合成了 C5aR N 端磷酸模拟物，并通过 ITC 和 NMR 研究了它们与金黄色葡萄球菌趋化抑制蛋白（CHIPS）的结合。与硫酸化形式相比，磷酸化的 C5aR 模拟物对 CHIPS 具有相当的结合亲和力和相似的结合模式。然而，在生物测定中，磷酸化肽的活性明显低于其硫酸化对应物。
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