Studies On The Synthesis Of Protein Tyrosine Phosphatases Based On The Mechanism

The protein tyrosine phosphatases (PTPs), which control the process of dephosphorylation of proteins,constitute a large family of signaling enzymes and play the key regulatory role during cell cycle.PTPs are linked to many diseases,including cancer, neurological disorders,and diabetes and so on. Thus,PTPs have been the promising targets for therapeutic intervention in recent years.In this thesis, we designed and synthesized fluorinated PTPs inhibitors and halogenated quinolone inhibitors based on the inhibitors of PTPs reported and the structure the PTPs'substrates.We hoped that they could specifically bond with a particular protein tyrosine phosphatase irreversibly. Conclusions and results were described below:1.After investigated different kinds of inhibitors of protein tyrosine phosphatases which had been synthesized successfully and combined with the structures of nature substrates of protein tyrosine phosphatases, our fluorinated protein tyrosine phosphatases inhibitors and halogenated quinolones inhibitors were designed and synthesized.2.In order to build our library of halogenated quinolones inhibitors for protein tyrosine phosphatases, we developed a general and efficient method to approach the important intermediate halogenated 2-quinolone.3.The activity tests of the halogenated 2-quinolone were carried out.