695171-98-3

Upstream product

• 149194-46-7 benzyl (4-amino-1-(diphenoxyphosphoryl)butyl)carbamate 
• 152120-54-2 (Z)-tert-butyl (((tert-butoxycarbonyl)imino)(1H-pyrazol-1-yl)methyl)carbamate 
• 621-84-1 O-benzyl carbamate 
• 149194-43-4 diphenyl benzyloxycarbonylamino-(3-phthalimidopropyl)methanephosphonate 
• 322474-21-5 N,N'-bis-Boc-S-methyl-isothiourea 
• 101-02-0 triphenyl phosphite 
• 152120-54-2 N,N'-bis( tert-butoxycarbonyl)-1H-pyrazole-1-carboxamidine 

Downstream Products

• 1005215-18-8 diphenyl N-(benzyloxycarbonylamino)-(3-guanidinopropyl)methanephosphonate trifluoroacetate 
• 695172-12-4 diphenyl ((N-benzyloxycarbonyl-O-tert-butyl-D-seryl)-L-alanyl)amino-(3-(N,N'-bis(tert-butyloxycarbonyl)guanyl)propyl)methanephosphonate 
• 695172-05-5 diphenyl (N-benzyloxycarbonyl-L-alanyl)amino-(3-(N,N'-bis(tert-butyloxycarbonyl)guanyl)propyl)methanephosphonate 

Relevant academic research and scientific papers

Compounds and methods for protease detection

Alternative methods for the detection and measurement of proteases in biological samples and compounds which allow for such detection are required to allow for rapid and selective identification of these enzymes. Compounds which allow for selective identification of these enzymes are provided with assays and kits for their use.

The first potent diphenyl phosphonate KLK4 inhibitors with unexpected binding kinetics

KLK4 is a serine protease from the kallikrein family that is involved in cancer progression. The diphenyl phosphonate warhead is intended to bind irreversibly with serine proteases, but unexpectedly, very potent KLK4 diphenyl phosphonate inhibitors were d

Development of Irreversible Diphenyl Phosphonate Inhibitors for Urokinase Plasminogen Activator

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.