Affinity-Guided Design of Caveolin-1 Ligands for Deoligomerization

被引：5

作者：

Gilliam, Amanda J. H. ^{[1
]}

Smith, Joshua N. ^{[2
]}

Flather, Dylan ^{[2
]}

Johnston, Kevin M. ^{[1
]}

Gansmiller, Andrew M. ^{[1
]}

Fishman, Dmitry A. ^{[1
]}

Edgar, Joshua M. ^{[1
]}

Balk, Mark ^{[1
,3
]}

Majumdar, Sudipta ^{[1
]}

Weiss, Gregory A. ^{[1
,2
]}

机构：

[1] Univ Calif Irvine, Dept Chem, Irvine, CA 92697 USA

[2] Univ Calif Irvine, Dept Mol Biol & Biochem, Irvine, CA 92697 USA

[3] Eindhoven Univ Technol, Den Dolech 2, NL-5612 AZ Eindhoven, Netherlands

来源：

JOURNAL OF MEDICINAL CHEMISTRY | 2016年 / 59卷 / 08期

关键词：

SPOT-SYNTHESIS; SCAFFOLDING DOMAIN; LIPID RAFTS; PROTEIN; BINDING; PEPTIDE; CELLS; CHOLESTEROL; PARALLEL; SUPPORT;

D O I：

10.1021/acs.jmedchem.5b01536

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

Caveoliu-1 is a target for academic and pharmaceutical research due to its many cellular roles and associated diseases. We report peptide W147 (1), a small, high-affinity, selective disrupter of caveolin-1 oligomers. Developed and optimized through screening and analysis of synthetic peptide libraries, ligand 1 has 7500 -fold improved affinity compared to its T20 parent ligand and an 80% decrease in sequence length. Ligand 1 will permit targeted study of caveoliri-1 function.

引用

页码：4019 / 4025

页数：7

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