42345-97-1

Basic information

• Product Name: C₁₁H₁₅Cl₃NO₃P
• Synonyms: C₁₁H₁₅Cl₃NO₃P
• CAS NO: 42345-97-1
• Molecular Weight: 346.578
• Mol File: 42345-97-1.mol
• Article Data: 6

Chemical Properties

• CAS DataBase Reference: C₁₁H₁₅Cl₃NO₃P(CAS DataBase Reference)
• NIST Chemistry Reference: C₁₁H₁₅Cl₃NO₃P(42345-97-1)
• EPA Substance Registry System: C₁₁H₁₅Cl₃NO₃P(42345-97-1)

Safety Data

• Hazardous Substances Data: 42345-97-1(Hazardous Substances Data)

Upstream product

• 127-88-8 N,N-di(2-chloroethyl)amidophosphoric acid dichloride 
• 1122-95-8 sodium 4-methoxyphenolate 
• 150-76-5 4-methoxy-phenol 

Downstream Products

• 83182-95-0 4-methoxyphenyl N,N-bis(2-chloroethyl)-N'-methylphosphorodiamidate 
• 1254975-86-4 C₂₆H₂₄Cl₂NO₇P 

Relevant articles and documents

Protease-mediated enzymatic hydrolysis and activation of aryl phosphoramidate derivatives of stavudine

Several proteases are capable of hydrolyzing the aryl substituted phosphoramidate derivatives of stavudine resulting in the formation of the active metabolite, alaninyl d4T monophosphate. Subtilisin Protease A, Subtilisin Griseus, Subtilisin Carlsberg, Papaya, Bacillus were amongst the most effective proteases in hydrolyzing stavudine derivatives and specificity of their activity was confirmed using several protease inhibitors to block the hydrolysis of these phosphoramidate derivatives. We found that these proteases exhibit chiral selectivity at the phosphorus center of stavudine derivatives. Our results indicate that cellular proteases may be responsible for the activation of these phosphoramidate derivatives. In addition, we show that the enzymatic hydrolysis takes place at the carboxymethyl ester side chain of these pro-drugs and the direct attack on the phosphorus center by these enzymes does not occur. Finally, we describe a novel activation pathway hitherto unknown for the activation and viral inhibitory characteristic shown by these phosphoramidate derivatives of stavudine.

Synthesis, cytotoxicity, topoisomerase I inhibition and molecular docking of novel phosphoramide mustard sophoridinic acid analogues

A series of novel phosphoramide mustard sophoridinic acid analogues, consisting of nitrogen mustard group and sophoridinic acid scaffold, have been designed, synthesized and evaluated for their topoisomerase inhibitory activity as well as cytotoxicity against six tumor cell lines (SMMC-7721, LoVo, MCF-7, K562, S180 and H22) and a normal cell line (L929). Among the compounds tested, five were found to be potent inhibitors and exhibited potent cytotoxicity against S180 and H22 cell lines with IC50 values of 1–4?μM. Further mechanistic studies showed that this class of compounds acted as novel topoisomerase I (Topo I) catalytic inhibitors by preventing the binding of Topo I to DNA and inhibiting the cleavage of DNA, and molecular docking studies revealed that the binding energy for these compounds was comparable to that for classic Topo I inhibitors CPT and HCPT, indicating that the compounds have an interaction with DNA and Topo I.

Lipase-mediated stereoselective hydrolysis of stampidine and other phosphoramidate derivatives of stavudine

Enzymatic hydrolysis of stampidine and other aryl phosphate derivatives of stavudine were investigated using the Candida Antarctica Type B lipase. Modeling studies and comparison of the hydrolysis rate constants revealed a chiral preference of the lipase