149194-47-8Relevant articles and documents
Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from plasmodium falciparum
Kannan Sivaraman, Komagal,Paiardini, Alessandro,Sieńczyk, Marcin,Ruggeri, Chiara,Oellig, Christine A.,Dalton, John P.,Scammells, Peter J.,Drag, Marcin,McGowan, Sheena
, p. 5213 - 5217 (2013/07/26)
The malaria parasite Plasmodium falciparum employs two metallo- aminopeptidases, PfA-M1 and PfA-M17, which are essential for parasite survival. Compounds that inhibit the activity of either enzyme represent leads for the development of new antimalarial drugs. Here we report the synthesis and structure-activity relationships of a small library of phosphonic acid arginine mimetics that probe the S1 pocket of both enzymes and map the necessary interactions that would be important for a dual inhibitor.
Development of Irreversible Diphenyl Phosphonate Inhibitors for Urokinase Plasminogen Activator
Joossens,Van Der Veken,Lambeir,Augustyns,Haemers
, p. 2411 - 2413 (2007/10/03)
In this letter we report the synthesis and biochemical evaluation of selective, irreversible diphenyl phosphonate inhibitors for urokinase plasminogen activator (uPA). A diphenyl phosphonate group was introduced on the substratelike peptide Z-D-Ser-Ala-Arg, and modification of the guanidine side chain was investigated. A guanylated benzyl group appeared the most promising side chain modification. A kapp value in the 103 M -1 s-1 range for uPA was obtained, together with a selectivity index higher than 240 toward other trypsin-like proteases such as tPA, thrombin, plasmin, and FXa.
A convenient synthesis of N-protected diphenyl phosphonate ester analogues of ornithine, lysine and homolysine
Hamilton,Walker,Walker
, p. 2847 - 2850 (2007/10/02)
A 3-step synthesis to the title compounds has been developed which provides them differentially protected at nitrogen. These could then be selectively deprotected using hydrazine hydrate or hydrogenolysis over Pd/C.