824970-16-3

Basic information

• Product Name: Carbamic acid, [2-oxo-2-[[6-oxo-6-(phenylamino)hexyl]amino]ethyl]-, 1,1-dimethylethyl ester
• CAS NO: 824970-16-3
• Molecular Formula: C19H29N3O4
• Molecular Weight: 363.457
• Mol File: 824970-16-3.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [2-oxo-2-[[6-oxo-6-(phenylamino)hexyl]amino]ethyl]-, 1,1-dimethylethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [2-oxo-2-[[6-oxo-6-(phenylamino)hexyl]amino]ethyl]-, 1,1-dimethylethyl ester(824970-16-3)
• EPA Substance Registry System: Carbamic acid, [2-oxo-2-[[6-oxo-6-(phenylamino)hexyl]amino]ethyl]-, 1,1-dimethylethyl ester(824970-16-3)

Safety Data

• Hazardous Substances Data: 824970-16-3(Hazardous Substances Data)

Upstream product

• 115012-32-3 N-[5-(phenylcarbamoyl)pentyl]carbamic acid benzyl ester 
• 62-53-3 aniline 
• 160777-08-2 7-oxo-7-(phenylamino)heptanoic acid 
• 111-16-0 heptanedioic acid 
• 4530-20-5 BOC-glycine 
• 115012-25-4 6-aminohexanoic acid phenylamide 

Relevant articles and documents

Novel inhibitors of human histone deacetylases: Design, synthesis, enzyme inhibition, and cancer cell growth inhibition of SAHA-based non-hydroxamates

To find novel non-hydroxamate histone deacetylase (HDAC) inhibitors, a series of compounds modeled after suberoylanilide hydroxamic acid (SAHA) was designed and synthesized. In this series, compound 7, in which the hydroxamic acid of SAHA is replaced by a thiol, was found to be as potent as SAHA, and optimization of this series led to the identification of HDAC inhibitors more potent than SAHA. In cancer cell growth inhibition assay, S-isobutyryl derivative 51 showed strong activity, and its potency was comparable to that of SAHA. The cancer cell growth inhibitory activity was verified to be the result of histone hyperacetylation and subsequent induction of p21WAF1/CIP1 by Western blot analysis. Kinetical enzyme assay and molecular modeling suggest the thiol formed by enzymatic hydrolysis within the cell interacts with the zinc ion in the active site of HDACs.