1363568-28-8Relevant academic research and scientific papers
Exploration of α-aminophosphonate N-derivatives as novel, potent and selective inhibitors of protein tyrosine phosphatases
Wang, Qingming,Zhu, Miaoli,Zhu, Ruiting,Lu, Liping,Yuan, Caixia,Xing, Shu,Fu, Xueqi,Mei, Yuhua,Hang, Qingwei
, p. 354 - 364 (2012)
Seventeen α-aminophosphonates are synthesized. Their compositions and structures are established by EA, UV, FT-IR, 1H NMR, 13C NMR, 31P NMR and ESI-MS. Compounds 1-4 are confirmed by X-ray crystallography. PTP inhibition shows compounds 1-5, 12, 15 are moderate competitive inhibitors with some selectivity. The most potent inhibitor is compound 5 with the lowest IC50 value about 6.64 μM against PTP1B, about 2-fold and 25-fold stronger than against TCPTP and PTP-MEG2 while it doesn't inhibit SHP-1 and SHP-2. The binding constant of 5 to PTP1B is 2.23 × 105 M-1 and binding ratio approximates 1:1. Cell viability and apoptosis assays indicate 5 is cell permeable with lower cytotoxicity. The results indicate α-aminophosphonates are possibly developed to effective and selective inhibitors of PTPs.
