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

doi:10.1016/j.bmcl.2012.10.054

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

Neurology

Research output: Contribution to journal › Article › peer-review

13 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 language	English (US)
Pages (from-to)	7440-7443
Number of pages	4
Journal	Bioorganic and Medicinal Chemistry Letters
Volume	22
Issue number	24
DOIs	https://doi.org/10.1016/j.bmcl.2012.10.054
State	Published - 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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10.1016/j.bmcl.2012.10.054

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

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.",

keywords = "Di-indolinone, Inhibitors, Molecular docking, Protein tyrosine phosphatase 1B",

author = "Dai, {Hou Ling} and Gao, {Li Xin} and Ying Yang and Li, {Jing Ya} and Cheng, {Jia Gao} and Jia Li and Ren Wen and Peng, {Yan Qing} and Zheng, {Jian Bin}",

note = "Funding Information: Project supports by National Natural Science Foundation of China (Grant No. 21102044 and Grant No. 21172070) and Shanghai Committee of Science and Technology (Grant No. 11DZ2260600). ",

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language = "English (US)",

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journal = "Bioorganic and Medicinal Chemistry Letters",

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T1 - Discovery of di-indolinone as a novel scaffold for protein tyrosine phosphatase 1B inhibitors

AU - Dai, Hou Ling

AU - Gao, Li Xin

AU - Yang, Ying

AU - Li, Jing Ya

AU - Cheng, Jia Gao

AU - Li, Jia

AU - Wen, Ren

AU - Peng, Yan Qing

AU - Zheng, Jian Bin

N1 - Funding Information: Project supports by National Natural Science Foundation of China (Grant No. 21102044 and Grant No. 21172070) and Shanghai Committee of Science and Technology (Grant No. 11DZ2260600).

PY - 2012/12/15

Y1 - 2012/12/15

N2 - 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.

AB - 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.

KW - Di-indolinone

KW - Inhibitors

KW - Molecular docking

KW - Protein tyrosine phosphatase 1B

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IS - 24

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

Abstract

Keywords

ASJC Scopus subject areas

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