178860-99-6Relevant articles and documents
Phosphonic analogues of glutamic acid as irreversible inhibitors of Staphylococcus aureus endoproteinase GluC: An efficient synthesis and inhibition of the human IgG degradation
Burchacka, Ewa,Skoreński, Marcin,Sieńczyk, Marcin,Oleksyszyn, Józef
, p. 1412 - 1415 (2013/03/28)
Endoproteinase GluC (V8 protease) is one of many virulence factors released by the Staphylococcus aureus species in vivo. The V8 protease is able to hydrolyze some serpins and all classes of mammalian immunoglobulins. The application of specific and potent inhibitors of V8 protease may lead to the development of new antibacterial agents. Herein, we present the synthesis and the inhibitory properties of novel peptidyl derivatives of a phosphonic glutamic acid analogue. One of the compounds Boc-Phe-Leu-GluP(OC 6H4)2 displayed an apparent second-order inhibition rate value of 8540 M-1 s-1. The Boc-Phe-Leu-GluP(OC6H4)2 compound with the highest inhibitory potency showed the ability to prevent V8-mediated human IgG proteolysis in vitro.
Towards the identification of unknown neuropeptide precursor-processing enzymes: Design and synthesis of a new family of dipeptidyl phosphonate activity probes for substrate-based protease identification
Sabidó, Eduard,Tarragó, Teresa,Giralt, Ernest
supporting information; experimental part, p. 8350 - 8355 (2011/02/22)
Specific proteolytic processing of inactive precursors is an exquisite cellular mechanism that triggers the activation of numerous physiologic peptides and proteins. This process ensures the generation of biologically active peptides, such as many neurope
Synthesis and proteinase inhibitory properties of diphenyl phosphonate analogues of aspartic and glutamic acids
Hamilton, Robert,Walker, Brian,Walker, Brian J.
, p. 1655 - 1660 (2007/10/03)
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.Asp(P)(OPh)2 and Acetyl.Glu(P)(OPh)2 were found to function as irreversible inactivators of V8 proteinase, yet exhibit no activity against granzyme B.
Synthesis of diphenyl phosphonate analogues of tyrosine and tryptophan and derived peptides as chymotrypsin inhibitors
Bergin, Carol,Hamilton, Robert,Walker, Brian,Walker, Brian J.
, p. 1155 - 1156 (2007/10/03)
The synthesis of α-aminophosphonate analogues of tyrosine and tryptophan, e.g. 4 and 5 respectively, and their incorporation into proline-containing dipeptides is reported; of the sequences synthesised, the dipeptide Z-Pro-Trp(P)(OPh)2 is the o
