Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1396183 | European Journal of Medicinal Chemistry | 2011 | 7 Pages |
With an aim of developing novel protein tyrosine phosphatase (PTP) 1B inhibitors based on sugar scaffolds, a focused library of benzyl 6-triazolo(hydroxy)benzoic glucosides was efficiently constructed via the modular and selective Cu(I)-catalyzed azide-alkyne 1,3-dipolar cycloaddtion (click chemistry). These glycoconjugates bearing alkyl chain length-varied bridges between the sugar and (hydroxy)-benzoic moieties were identified as new PTP1B inhibitors with selectivity over T-Cell PTP (TCPTP), SH2-Containing PTP-1 (SHP-1), SHP-2 and Leukocyte Antigen-Related Tyrosine Phosphatase (LAR). Molecular docking study sequentially elaborated the plausible binding modes of the structurally diverse sugar-based inhibitors with PTP1B.
Graphical abstractNovel PTP1B inhibitors based on a sugar scaffold were efficiently constructed via click chemistry. Molecular docking study sequentially elaborated their plausible binding modes with PTP1B.Figure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Novel PTP1B inhibitors based on a glucosyl scaffold were developed. ► Click chemistry was employed to modularly construct the focused library. ► The inhibitors were identified with high selectivity on PTP1B over others. ► Plausible PTP1B inhibitor interactions were suggested by molecular docking.