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Bioorg Med Chem Lett. 2012 Dec 15;22(24):7440-3. doi: 10.1016/j.bmcl.2012.10.054. Epub 2012 Oct 17.

Discovery of di-indolinone as a novel scaffold for protein tyrosine phosphatase 1B inhibitors.

Author information

1
Shanghai Key Laboratory of New Drug Design, School of Pharmacy, East China University of Science and Technology, Shanghai 200237, PR China.

Abstract

A series of di-indolinone derivatives was designed and synthesized to optimize our lead compounds basing on molecular docking study as PTP1B inhibitors. Successive enzymatic assay identified the synthetic di-indolinone as novel PTP1B inhibitors with low micromole-ranged inhibitory activity and at least several-fold selectivity over other tested homologous PTPs.

PMID:
23122522
DOI:
10.1016/j.bmcl.2012.10.054
[Indexed for MEDLINE]

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