Novel hydroxamic acid-related phosphinates: inhibition of neutral aminopeptidase N (APN).
Here we describe the inhibitory activity toward neutral aminopeptidase of three new families of phosphinate inhibitors related in structure to hydroxamic acids. These compounds, even as racemic mixtures, are good inhibitors of APN and show strong structure activity relationship (SAR) depending on the substituents in P1 and P1' positions.
Drag
Marcin
M
Division of Medicinal Chemistry and Microbiology, Faculty of Chemistry, Wroclaw University of Technology, Wybrzeze Wyspianskiego 27, 50-370 Wroclaw, Poland. mdrag@burnham.org
Grzywa
Renata
R
Oleksyszyn
Jozef
J
D001667:Binding, Competitive / Q000187:drug effects; D018826:CD13 Antigens / Q000037:antagonists & inhibitors*; D004791:Enzyme Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology*; D006877:Hydroxamic Acids / Q000138:chemical synthesis* / Q000494:pharmacology*; D007700:Kinetics; D045726:Metalloproteases / Q000037:antagonists & inhibitors; D010721:Phosphinic Acids / Q000138:chemical synthesis* / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000138:chemical synthesis / Q000494:pharmacology; D013237:Stereoisomerism
D004791:Enzyme Inhibitors; D006877:Hydroxamic Acids; D010721:Phosphinic Acids; D011480:Protease Inhibitors; D045726:Metalloproteases; D018826:CD13 Antigens