alpha-Bromoacetophenone derivatives as neutral protein tyrosine phosphatase inhibitors: Structure-activity relationship

Abstract

A series of α-haloacetophenone derivatives was tested for inhibition of protein tyrosine phosphatases SHP-1 and PTP1B. The results show that the bromides are much more potent than the corresponding chlorides, whereas the phenyl ring is remarkably tolerant to modifications. Derivatization of the phenyl ring with a tripeptide Gly-Glu-Glu resulted in a potent, selective inhibitor against PTP1B.

A series of α-haloacetophenone derivatives was tested against SHP-1 and PTB1B to define the SAR.