Structure-Activity Relationship Study of Cyclic Pentapeptide Ligands for Atypical Chemokine Receptor 3 (ACKR3)

被引：3

作者：

Sekiguchi, Haruka ^{[1
]}

Kuroyanagi, Tomoko ^{[1
]}

Rhainds, David ^{[2
,3
]}

Kobayashi, Kazuya ^{[4
]}

Kobayashi, Yuka ^{[1
]}

Ohno, Hiroaki ^{[1
]}

Heveker, Nikolaus ^{[2
,3
]}

Akaji, Kenichi ^{[4
]}

Fujii, Nobutaka ^{[1
]}

Oishi, Shinya ^{[1
]}

机构：

[1] Kyoto Univ, Grad Sch Pharmaceut Sci, Sakyo Ku, Kyoto 6068501, Japan

[2] Univ Montreal, Dept Biochim, Montreal, PQ H3T 1J4, Canada

[3] Univ Montreal, St Justine Hosp, Res Ctr, Montreal, PQ H3T 1C5, Canada

[4] Kyoto Pharmaceut Univ, Yamashina Ku, Kyoto 6078412, Japan

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2018年 / 61卷 / 08期

基金：

加拿大健康研究院;

关键词：

CXCR4/CXCR7/CXCL12; PATHWAY; CXCR4; ANTAGONISTS; PROSTATE-CANCER; MIGRATION; CXCL12/SDF-1; TC14012; GROWTH; CELLS; RDC1;

D O I：

10.1021/acs.jmedchem.8b00336

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

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-MeArgL-Nal(2)-L-Pro-)], for the development of highly active ACKR3 ligands. Notably, modification at the L-Pro position with toward ACKR3. a bulky hydrophobic side chain led to improved bioactivity toward ACKR3.

引用

页码：3745 / 3751

页数：7

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