467468-18-4

Upstream product

• 2759-28-6 1-phenylmethylpiperazine 
• 110-85-0 piperazine 
• 219311-20-3 5-(4-phenoxyphenyl)pyrimidine-2,4,6-trione 
• 14199-15-6 Methyl 4-hydroxyphenylacetate 
• 4664-61-3 methyl [p-(phenoxy)phenyl]acetate 
• 288103-00-4 dimethyl 2-(4-phenoxyphenyl)malonate 
• 98-80-6 phenylboronic acid 

Downstream Products

• 467468-14-0 4-Oxo-4,4-[2,4,6-trioxo-5-(4-phenoxy-phenyl)-hexahydro-pyrimidin-5-yl]-piperazin-1-yl-butyric acid 
• 1233817-00-9 5-[4-(2-[18F]fluoroethyl)piperazin-1-yl]-5-(4-phenoxyphenyl)pyrimidine-2,4,6-trione 
• 1333167-73-9 5-(4-(thiophene-2-carbonyl)piperazin-1-yl)-5-(4-phenoxyphenyl)pyrimidine-2,4,6(1H,3H,5H)-trione 

Relevant academic research and scientific papers

N-Substituted homopiperazine barbiturates as gelatinase inhibitors

Matrix metalloproteinases are implicated in a wide range of pathophysiological processes and potent selective inhibitors for these enzymes continue to be eagerly sought. 5,5-Disubstituted barbiturates hold promise as inhibitor types being stable in vivo and relatively selective for the gelatinases (MMP-2 and MMP-9). In this paper we describe the synthesis of 5-piperazine and -homopiperazine substituted barbiturates. The activity of these compounds as gelatinase inhibitors was evaluated using supernatants from 12-O-tetradecanoylphorbol-13-acetate (PMA)-stimulated HT-1080 cells as well as using recombinant human MMPs. N-Acyl homopiperazine compounds were found to be potent inhibitors of the gelatinases (range in nM) and generally more potent than the corresponding piperazine analogues. The panel of N-acyl homopiperazines was enlarged in order to exploit differences between the gelatinases at the S2′ site in order to design MMP-2- or MMP-9-selective inhibitors. Compounds in this group exhibited single digit nano-molar potency and some selectivity between the two enzymes. Representative potent compounds were effective inhibitors of cancer cell migration.

Radiofluorinated pyrimidine-2,4,6-triones as molecular probes for noninvasive MMP-targeted imaging

Matrix metalloproteinases (MMPs) are zinc- and calcium-dependent endopeptidases. Representing a subfamily of the metzincin superfamily, MMPs are involved in the proteolytic degradation of components of the extracellular matrix. Unregulated MMP expression,

Barbituric acid derivatives

Derivatives of 5,5-disubstituted pyrimidine-2,4,6-trianones are disclosed. These compounds have antitumor and antimetastatic activity.