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

Hou Ling Dai, Li Xin Gao, Ying Yang, Jing Ya Li, Jia Gao Cheng*, Jia Li, Ren Wen, Yan Qing Peng, Jian Bin Zheng

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)7440-7443
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume22
Issue number24
DOIs
StatePublished - Dec 15 2012

Keywords

  • Di-indolinone
  • Inhibitors
  • Molecular docking
  • Protein tyrosine phosphatase 1B

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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