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Discovery of novel selenium derivatives as Pin1 inhibitors by high-throughput screening.

Abstract：

:Peptidyl prolyl cis/trans isomerization by Pin1 regulates various oncogenic signals during cancer progression, and its inhibition through multiple approaches has established Pin1 as a therapeutic target. However, lack of simplified screening systems has limited the discovery of potent Pin1 inhibitors. We utilized phosphorylation-dependent binding of Pin1 to its specific substrate to develop a screening system for Pin1 inhibitors. Using this system, we screened a chemical library, and identified a novel selenium derivative as Pin1 inhibitor. Based on structure-activity guided chemical synthesis, we developed more potent Pin1 inhibitors that inhibited cancer cell proliferation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Subedi A,Shimizu T,Ryo A,Sanada E,Watanabe N,Osada H

doi

10.1016/j.bbrc.2016.04.124

subject

Has Abstract

pub_date

2016-06-03 00:00:00

pages

528-533

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(16)30638-6

journal_volume

474

pub_type

杂志文章

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