期刊
BIOORGANIC CHEMISTRY
卷 80, 期 -, 页码 195-203出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bioorg.2018.06.008
关键词
Flavonoid; Azole; Protein tyrosine phosphatase; Selectivity; Cell viability
资金
- Natural Science Foundation of the Jiangsu Higher Education Institutions of China [17KJB150041]
- Practice Inovation Trainng Program Projects for the Jiangsu College students [201710324004X, 201710324020Z, 201710324126C]
A series of azolyl flavonoids were synthesized and characterized by NMR, IR, MS and HAMS spectra. All the newly prepared compounds were screened for their potential protein tyrosine phosphatase inhibitory activities. Bioactive assay manifested that most of the azolyl flavonoids exhibited good protein phosphatase 1B (PTP1B) inhibitory activities. Especially, triazolyl flavonoid 6a displayed the best inhibitory activity (IC50 = 1.6 mu M) with 9.9-fold selectivity for PTP1B over the closely related T-cell protein tyrosine phosphatase (TCPTP). Cell viability assays indicated 6a has lower cytotoxicity. Molecular modeling and dynamics studies revealed the reason of selectivity for PTP1B over TCPTP. Quantum chemical studies were carried out on these compounds to understand the structural features essential for activity.
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