Synthesis and proteinase inhibitory properties of diphenyl phosphonate analogues of aspartic and glutamic acids.
The synthesis of diphenyl phosphonate analogues of aspartic and glutamic acid, and their inhibitory activity against S. aureus V8 protease and granzyme B, is described. The study has revealed difficulties with protecting group compatibility in the synthesis of these analogues. Two analogues, Acetyl. AspP (OPh)2 and Acetyl.GluP (OPh)2 were found to function as irreversible inactivators of V8 proteinase, yet exhibit no activity against granzyme B.
Hamilton
R
R
School of Chemistry, Queen's University of Belfast, Northern Ireland.
Walker
B
B
Walker
B J
BJ
D001224:Aspartic Acid / Q000031:analogs & derivatives*; D002384:Catalysis; D018698:Glutamic Acid / Q000031:analogs & derivatives*; D006868:Hydrolysis; D007700:Kinetics; D063065:Organophosphonates / Q000138:chemical synthesis* / Q000494:pharmacology*; D011480:Protease Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology*; D012697:Serine Endopeptidases / Q000187:drug effects / Q000378:metabolism
D063065:Organophosphonates; D011480:Protease Inhibitors; D001224:Aspartic Acid; D018698:Glutamic Acid; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase