168749-30-2

Basic information

• Product Name: (R)-NIPECOTAMIDE
• Synonyms: (R)-NIPECOTAMIDE;(3R)-Piperidine-3-carboxamide;(3R)-3-Piperidinecarboxamide;(R)-Piperidine-3-carboxylic acid amide;(R)-Piperidine-3-carboxamide
• CAS NO: 168749-30-2
• Molecular Formula: C6H12N2O
• Molecular Weight: 128.17228
• Mol File: 168749-30-2.mol
• Article Data: 12

Chemical Properties

• Boiling Point: 311.7±31.0 °C(Predicted)
• Appearance: /
• Density: 1.060±0.06 g/cm3(Predicted)
• Storage Temp.: under inert gas (nitrogen or Argon) at 2–8 °C
• PKA: 16.50±0.20(Predicted)
• CAS DataBase Reference: (R)-NIPECOTAMIDE(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-NIPECOTAMIDE(168749-30-2)
• EPA Substance Registry System: (R)-NIPECOTAMIDE(168749-30-2)

Safety Data

• Hazardous Substances Data: 168749-30-2(Hazardous Substances Data)

Usage

General Description

(R)-NIPECOTAMIDE is a chemical compound that belongs to the family of nipecotic acid derivatives. It is an enantiomer of nipecotic acid, which is a GABA reuptake inhibitor used for its potential therapeutic effects on epilepsy and other neurological disorders. (R)-NIPECOTAMIDE has been shown to have similar pharmacological properties to nipecotic acid, including its ability to inhibit GABA reuptake, and it has been studied for its potential use in the treatment of epilepsy and other related conditions. Additionally, (R)-NIPECOTAMIDE has been investigated for its potential as an anxiolytic and anticonvulsant agent, showing promise as a possible candidate for the development of new pharmaceuticals for neurological disorders.

Upstream product

• 7032-11-3 1,4,5,6-tetrahydropyridine-3-carboxamide 
• 98-92-0 nicotinamide 
• 4138-26-5 nipecotamide 
• 25334-23-0 nicotinamide hydrochloride 
• 1262398-24-2 R-nipecotamide D-lactic acid 

Downstream Products

• 94379-05-2 (R,S)-N-benzylpiperidine-3-carboxamide 
• 915226-43-6 (R)-tert-butyl 3-carbamoylpiperidine-1-carboxylate 
• 498-95-3 (S)-nipecotic acid 
• 88495-55-0 (S)-piperidine-3-carboxamide 
• 498-95-3 (R)-nipecotic acid 
• 142643-29-6 tert-butyl (piperidin-3-ylmethyl)carbamate 

Relevant articles and documents

A mild and facile method for complete hydrogenation of aromatic nuclei in water

A mild and complete hydrogenation of aromatic rings catalyzed by heterogeneous 10% Rh/C proceeds at 80 °C in water under 5 atm of H 2 pressure. This method is applicable to the hydrogenation of various carbon and heteroaromatic compounds such as alkylbenzenes, biphenyls, pyridines and furans. Georg Thieme Verlag Stuttgart.

A General Catalyst Based on Cobalt Core–Shell Nanoparticles for the Hydrogenation of N-Heteroarenes Including Pyridines

Herein, we report the synthesis of specific silica-supported Co/Co3O4 core–shell based nanoparticles prepared by template synthesis of cobalt-pyromellitic acid on silica and subsequent pyrolysis. The optimal catalyst material allows for general and selective hydrogenation of pyridines, quinolines, and other heteroarenes including acridine, phenanthroline, naphthyridine, quinoxaline, imidazo[1,2-a]pyridine, and indole under comparably mild reaction conditions. In addition, recycling of these Co nanoparticles and their ability for dehydrogenation catalysis are showcased.

Characterization of an enantioselective amidase from Cupriavidus sp. KNK-J915 (FERM BP-10739) useful for enzymatic resolution of racemic 3-piperidinecarboxamide

A novel amidase (CsAM) acting on (R,S)-N-benzyl-3-piperidinecarboxamide was purified from Cupriavidus sp. KNK-J915 (FERM BP-10739) and characterized. The enzyme acts on (R,S)-N-benzyl-3-piperidinecarboxamide S-selectively to yield (R)-N-benzyl-3-piperidinecarboxamide. Analytical gel filtration column chromatography and SDS-PAGE revealed that the enzyme is a tetramer with a subunit of approximately 47 kDa. It has a broad substrate spectrum against nitrogen-containing heterocyclic amides. Its optimal pH and temperature are 8.0-9.0 and 50 °C, respectively. The CsAM gene was cloned and sequenced, and it was found to comprise 1341 bp and encode a polypeptide of 46,388 Da. The deduced amino acid sequence exhibited 78% identity to that of a putative amidase (CnAM) from Cupriavidus necator JMP134. The cultured cells of recombinant Escherichia coli producing CnAM could be used for the S-selective hydrolysis of (R,S)-N-benzyl-3-piperidinecarboxamide but could not be used for the S-selective hydrolysis of (R,S)-3-piperidinecarboxamide because of its very low level of selectivity. In contrast, the cultured cells of recombinant E. coli producing CsAM could hydrolyze both (R,S)-N-benzyl-3-piperidinecarboxamide and (R,S)-3-piperidinecarboxamide with high S-selectivity.