alpha-bromoacetophenone derivatives as neutral protein tyrosine phosphatase inhibitors: structure-Activity relationship.
A series of alpha-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.
Arabaci
Gulnur
G
Department of Chemistry and Ohio State Biochemistry Program, The Ohio State University, 100 West 18th Avenue, Columbus, OH 43210, USA.
Yi
Tian
T
Fu
Hua
H
Porter
Mary E
ME
Beebe
Kirk D
KD
Pei
Dehua
D
D000098:Acetophenones / Q000138:chemical synthesis* / Q000494:pharmacology*; D001665:Binding Sites; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D007202:Indicators and Reagents; D007700:Kinetics; D010455:Peptides / Q000138:chemical synthesis / Q000494:pharmacology; D017027:Protein Tyrosine Phosphatases / Q000037:antagonists & inhibitors* / Q000737:chemistry; D013329:Structure-Activity Relationship
D000098:Acetophenones; D004791:Enzyme Inhibitors; D007202:Indicators and Reagents; D010455:Peptides; C013190:phenacyl bromide; D017027:Protein Tyrosine Phosphatases