149648-52-2

Basic information

• Product Name: 7-Phenylcarbamoylheptanoic acid
• Synonyms: Octanoic acid,8-oxo-8-(phenylamino)-;8-Oxo-8-(phenylamino);7-PHENYLCARBAMOYL-HEPTANOIC ACID;8-Oxo-8-(phenylamino)octanoic acid
• CAS NO: 149648-52-2
• Molecular Formula: C₁₄H₁₉NO₃
• Molecular Weight: 249.31
• Product Categories: Aromatics;Intermediates & Fine Chemicals;Pharmaceuticals
• Mol File: 149648-52-2.mol
• Article Data: 36

Chemical Properties

• Melting Point: 123°C
• Boiling Point: 488.556 °C at 760 mmHg
• Flash Point: 249.27 °C
• Appearance: /
• Density: 1.153
• Vapor Pressure: 0mmHg at 25°C
• Refractive Index: 1.56
• Storage Temp.: Refrigerator
• PKA: 4.78±0.10(Predicted)
• CAS DataBase Reference: 7-Phenylcarbamoylheptanoic acid(CAS DataBase Reference)
• NIST Chemistry Reference: 7-Phenylcarbamoylheptanoic acid(149648-52-2)
• EPA Substance Registry System: 7-Phenylcarbamoylheptanoic acid(149648-52-2)

Safety Data

• Hazardous Substances Data: 149648-52-2(Hazardous Substances Data)

Usage

Chemical Properties

White Solid

Uses

An intermediate in the production of Suberoylanilide Hydroxamic Acid and other histone deacetylase inhibitors

InChI:InChI=1/C14H19NO3/c16-13(15-12-8-4-3-5-9-12)10-6-1-2-7-11-14(17)18/h3-5,8-9H,1-2,6-7,10-11H2,(H,15,16)(H,17,18)

Upstream product

• 14354-86-0 suberic dianilide 
• 3946-32-5 suberic acid monomethyl ester 
• 62-53-3 aniline 
• 5698-29-3 oxonan-2-one 
• 162853-41-0 8-oxo-8-(phenylamino)octanoic acid methyl ester 
• 505-48-6 octane-1,8-dioic acid 
• 41624-92-4 methyl 8-chloro-8-oxooctanoate 
• 10521-06-9 oxonane-2,9-dione 

Downstream Products

• 149647-78-9 vorinostat 

Relevant articles and documents

Platinum(IV) prodrugs multiply targeting genomic DNA, histone deacetylases and PARP-1

Several Pt(IV) prodrugs containing SAA, a histone deacetylases inhibitor, were designed and prepared for multiply targeting genomic DNA, histone deacetylases and PARP-1. The resulting Pt(IV) prodrug had significantly strong antiproliferative activity against the tested cancer cell lines, especially SAA1, derived from the conjugation of cisplatin and SAA, had potent ability to overcome cisplatin resistance. Under the combined action of DNA platination and inhibition of HDACs and PARP-1 activity, the cytotoxic activity of SAA1 was 174-fold higher than cisplatin against cisplatin-resistant SGC7901/CDDP cancer cells. The mechanism of action of SAA1 was preliminarily investigated, in which cellular uptake, cell apoptosis and cell cycle arrest as well as western blot analysis were made by treating SAA1 with SGC7901/CDDP cells. Besides, HDACs inhibition activity and PARP-1 enzyme inhibition of SAA1 were also studied.

Hypoxia-activated pro-drugs of the KDAC inhibitor vorinostat (SAHA)

Hypoxia (lower than normal oxygen) is a characteristic of most solid tumours that results in poor cancer patient prognosis. The difference in cellular environment between normoxia (21percent oxygen) or physoxia (4–7.5percent oxygen) and hypoxia (2.0percent oxygen) causes increased resistance to radio- and chemotherapy, but also provides the opportunity to selectively release hypoxia-activated pro-drugs. This approach potentially allows targeting of chemotherapies, including lysine deacetylase (KDAC) inhibitors, to the hypoxic fraction of cells. Here, we report initial work on the development of KDAC inhibitors that are selectively released in hypoxic conditions. We have shown that the addition of a 4-nitrobenzyl (NB) or 1-methyl-2-nitroimidazole (NI) bioreductive group onto the hydroxamic acid moiety of SAHA, giving NB-SAHA and NI-SAHA, abolishes KDAC inhibition activity. Both NB-SAHA and NI-SAHA undergo enzyme-mediated bioreduction, in a hypoxia-dependent manner, to release SAHA selectively in 0.1percent oxygen. This work provides an important foundation for further investigations into the targeted release of KDAC inhibitors in hypoxic tumours.

The involvement of the mitochondrial amidoxime reducing component (MARC) in the reductive metabolism of hydroxamic acidsS

The mitochondrial amidoxime reducing component is a recently discovered molybdenum enzyme in mammals which, in concert with the electron transport proteins cytochrome b5 and NADH cytochrome b5 reductase, catalyzes the reduction of N-oxygenated structures.