环状五肽配体对非典型趋化因子受体 3（ACKR3）的构效关系研究。
Structure-Activity Relationship Study of Cyclic Pentapeptide Ligands for Atypical Chemokine Receptor 3 (ACKR3).
机构信息
Graduate School of Pharmaceutical Sciences , Kyoto University , Sakyo-ku, Kyoto 606-8501 , Japan.
Département de Biochimie , Université de Montréal , Montréal H3T 1J4 , Canada.
出版信息
J Med Chem. 2018 Apr 26;61(8):3745-3751. doi: 10.1021/acs.jmedchem.8b00336. Epub 2018 Apr 12.
The atypical chemokine receptor 3 (ACKR3)/CXC chemokine receptor 7 (CXCR7) recognizes stromal cell-derived factor 1 (SDF-1)/CXCL12 and is involved in a number of physiological and pathological processes. Here, we investigated the SAR of the component amino acids in an ACKR3-selective ligand, FC313 [ cyclo(-d-Tyr-l-Arg-l-MeArg-l-Nal(2)-l-Pro-)], for the development of highly active ACKR3 ligands. Notably, modification at the l-Pro position with a bulky hydrophobic side chain led to improved bioactivity toward ACKR3.
非典型趋化因子受体 3（ACKR3）/CXC 趋化因子受体 7（CXCR7）识别基质细胞衍生因子 1（SDF-1）/CXCL12，并参与许多生理和病理过程。在这里，我们研究了 ACKR3 选择性配体 FC313 [cyclo（-d-Tyr-l-Arg-l-MeArg-l-Nal（2）-l-Pro-）]中组成氨基酸的 SAR，以开发高活性的 ACKR3 配体。值得注意的是，在 l-Pro 位置用大体积的疏水侧链进行修饰，导致对 ACKR3 的生物活性提高。
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