913239-29-9Relevant articles and documents
Phosphonate inhibitors of West Nile virus NS2B/NS3 protease
Skoreński, Marcin,Milewska, Aleksandra,Pyr?, Krzysztof,Sieńczyk, Marcin,Oleksyszyn, Józef
, p. 8 - 14 (2019)
West Nile virus (WNV) is a member of the flavivirus genus belonging to the Flaviviridae family. The viral serine protease NS2B/NS3 has been considered an attractive target for the development of anti-WNV agents. Although several NS2B/NS3 protease inhibitors have been described so far, most of them are reversible inhibitors. Herein, we present a series of α-aminoalkylphosphonate diphenyl esters and their peptidyl derivatives as potent inhibitors of the NS2B/NS3 protease. The most potent inhibitor identified was Cbz-Lys-Arg-(4-GuPhe)P(OPh)2 displaying Ki and k2/Ki values of 0.4 μM and 28 265 M?1s?1, respectively, with no significant inhibition of trypsin, cathepsin G, and HAT protease.
Novel Urokinase Inhibitors
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Page/Page column 28; 30; 36, (2009/01/24)
The present invention relates to novel compounds with inhibitory activity towards urokinase plasminogen activator (uPA); to methods for preparation of said uPA inhibitor compounds; to pharmaceutical compositions comprising said uPA inhibitor compounds; to
Small, potent, and selective diaryl phosphonate inhibitors for urokinase-type plasminogen activator with in vivo antimetastatic properties
Joossens, Jurgen,Ali, Omar M.,El-Sayed, Ibrahim,Surpateanu, Georgiana,Der Van Veken, Pieter,Lambeir, Anne-Marie,Setyono-Han, Buddy,Foekens, John A.,Schneider, Anneliese,Schmalix, Wolfgang,Haemers, Achtel,Augustyns, Koen
, p. 6638 - 6646 (2008/09/17)
A set of small nonpeptidic diaryl phosphonate inhibitors was prepared. Some of these inhibitors show potent and highly selective irreversible uPA inhibition. The biochemical and modeling data prove that the combination of a benzylguanidine moiety with a d
A p-[18F]fluoroethoxyphenyl bicyclic nucleoside analogue as a potential positron emission tomography imaging agent for varicella-zoster virus thymidine kinase gene expression
Chitneni, Satish K.,Deroose, Christophe M.,Balzarini, Jan,Gijsbers, Rik,Celen, Sofie,Debyser, Zeger,Mortelmans, Luc,Verbruggen, Alfons M.,Bormans, Guy M.
, p. 6627 - 6637 (2008/09/17)
We recently reported a new positron emission tomography (PET) reporter gene, namely, varicella-zoster virus thymidine kinase (VZV-tk) in combination, with carbon-11 or fluorine-18 labeled m-alkoxyphenyl bicyclic nucleoside analogues (BCNAs) as PET reporte
NOVEL UROKINASE INHIBITORS
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Page/Page column 81-82; 84; 86, (2010/11/27)
The present invention relates to novel compounds with inhibitory activity towards urokinase plasminogen activator (uPA); to methods for preparation of said uPA inhibitor compounds; to pharmaceutical compositions comprising said uPA inhibitor compounds; to
Diphenyl phosphonate inhibitors for the urokinase-type plasminogen activator: Optimization of the P4 position
Joossens, Jurgen,Van Der Veken, Pieter,Surpateanu, Georgiana,Lambeir, Anne-Marie,El-Sayed, Ibrahim,Ali, Omar M.,Augustyns, Koen,Haemers, Achiel
, p. 5785 - 5793 (2007/10/03)
This paper describes the structure-activity relationship in a series of tripeptidyl diphenyl phosphonate irreversible urokinase plasminogen activator (uPA) inhibitors, originally derived from an arginyltripeptide. uPA is considered an interesting target i
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.