Literature

Abstract

In this study, we describe the design, synthesis, biological evaluation and molecular modelling studies of novel non-carboxylic arylidine malononitrile-based molecules as Protein Tyrosine Phosphatase 1B (PTP1B) inhibitors. The synthesized derivatives were evaluated in vitro for glucose reuptake using L6 muscle cell lines and enzymatic assay against PTP1B. The biological activity results showed that the 2-methoxy substituted (14b) compound exhibited significant activity in both the assays. The unsubstituted compound (14a) also possessed comparable activity on glucose reuptake in L6 muscle cell lines and better inhibitory activity on PTP1B enzyme assays.

DOI： 10.1007/s00044-013-0528-1

Design, synthesis and biological evaluation of novel arylidine-malononitrile derivatives as non-carboxylic inhibitors of protein tyrosine phosphatase 1B

Medicinal Chemistry Research 2013.0

Design, synthesis and docking studies on phenoxy-3-piperazin-1-yl-propan-2-ol derivatives as protein tyrosine phosphatase 1B inhibitors

Bioorganic & Medicinal Chemistry Letters 2010.0

Molecular modeling and synthesis of ZINC02765569 derivatives as protein tyrosine phosphatase 1B inhibitors: lead optimization study

Medicinal Chemistry Research 2013.0

Identification of novel urea derivatives as PTP1B inhibitors: synthesis, biological evaluation and structure–activity relationships

MedChemComm 2013.0

Novel Imbricatolic acid derivatives as protein tyrosine phosphatase-1B inhibitors: Design, synthesis, biological evaluation and molecular docking

Bioorganic & Medicinal Chemistry Letters 2016.0

Synthesis, in vitro and computational studies of protein tyrosine phosphatase 1B inhibition of a small library of 2-arylsulfonylaminobenzothiazoles with antihyperglycemic activity