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Usage

Uses

Used in Pharmaceutical Industry:
5-(Benzoylamino)valeric acid is used as a building block for the synthesis of pharmaceuticals due to its unique chemical structure and properties. It can be incorporated into the development of new drugs, potentially enhancing their efficacy and therapeutic outcomes.
Used in Agrochemical Industry:
In the agrochemical industry, 5-(Benzoylamino)valeric acid is utilized as a building block for the synthesis of agrochemicals. Its unique properties can contribute to the development of novel compounds with improved performance in agricultural applications.
Used in Organic Compounds Synthesis:
5-(Benzoylamino)valeric acid is used as a building block in the synthesis of various organic compounds. Its unique structure allows for the creation of new materials with potential applications in different industries, such as chemical manufacturing and research.
Used in Drug Development:
5-(Benzoylamino)valeric acid has potential applications in the development of new drugs. Its unique chemical properties can be leveraged to design and synthesize innovative pharmaceutical compounds with improved therapeutic effects and reduced side effects.
Used in Material Development:
Due to its unique chemical structure, 5-(Benzoylamino)valeric acid can be used in the development of new materials. It can contribute to the creation of innovative materials with enhanced properties, such as improved stability, reactivity, or selectivity, for use in various applications.

InChI:InChI=1/C12H15NO3/c14-11(15)8-4-5-9-13-12(16)10-6-2-1-3-7-10/h1-3,6-7H,4-5,8-9H2,(H,13,16)(H,14,15)

Upstream product

• 776-75-0 N-benzoylpiperidine 
• 100253-61-0 5-benzoylamino-valeric acid amide 
• 98-88-4 benzoyl chloride 
• 660-88-8 5-aminopentanoic acid 
• 63984-02-1 methyl 5-aminovalerate 
• 65-85-0 benzoic acid 
• 101115-37-1 5-benzoylamino-valeric acid ethyl ester 
• 29840-57-1 5-aminovaleric acid ethyl ester hydrochloride 
• 675-20-7 piperidin-2-one 
• 110-89-4 piperidine 
• 857488-39-2 4-benzamidobutyl iodide 
• 5107-18-6 N⁶-benzoyl-lysine 
• 6066-84-8 5-N-benzamidopentanenitrile 
• 4252-56-6 1-benzoylpiperidin-2-one 

Downstream Products

• 101115-37-1 5-benzoylamino-valeric acid ethyl ester 
• 675-20-7 piperidin-2-one 
• 65-85-0 benzoic acid 
• 57050-07-4 2-phenyl-3,4,5,6-tetrahydropyridine 
• 69980-44-5 N⁵-benzoyl-DL-ornithine 
• 43218-39-9 5-benzoylamino-valeryl chloride 
• 102303-88-8 5-benzoylamino-valeric acid anilide 
• 609-36-9 rac-Pro-OH 
• 17079-25-3 methyl N-benzoyl-5-aminopentanoate 
• 3326-13-4 N-acetyl-2-piperidone 
• 5692-23-9 N-(4-aminobutyl)benzamide 
• 31991-78-3 uvariadiamide 
• 100253-61-0 5-benzoylamino-valeric acid amide 

Relevant academic research and scientific papers

Synthetic studies towards N-substituted 3-vinyl-4-piperidineacetic acid derivatives

The synthesis and full characterization of two new (E)-2-butenyl)-5-amino-2-pentenoates, (Z)-4-[N-(3-buten-1-yl)benzamido]-2-buten-1-ol, and (Z)-1-chloro-4-[N-(3-buten-l-yl)benzamido]-2-butene are reported. These were designed as substrates for a projected thermal ene cyclization leading to the N-substituted 3-vinyl-4-piperidineacetic acid scaffold. Although conditions for this ene-cyclization have not yet been uncovered, the ease of preparation of these ene-cyclization substrates gives promise for their future use.

Directing Group in Decarboxylative Cross-Coupling: Copper-Catalyzed Site-Selective C-N Bond Formation from Nonactivated Aliphatic Carboxylic Acids

Copper-catalyzed directed decarboxylative amination of nonactivated aliphatic carboxylic acids is described. This intramolecular C-N bond formation reaction provides efficient access to the synthesis of pyrrolidine and piperidine derivatives as well as the modification of complex natural products. Moreover, this reaction presents excellent site-selectivity in the C-N bond formation step through the use of directing group. Our work can be considered as a big step toward controllable radical decarboxylative carbon-heteroatom cross-coupling.

A metabolic screening study of trichostatin A (TSA) and TSA-like histone deacetylase inhibitors in rat and human primary hepatocyte cultures

Hydroxamic acid (HA)-based histone deacetylase (HDAC) inhibitors, with trichostatin A (TSA) as the reference compound, are potential antitumoral drugs and show promise in the creation of long-term primary cell cultures. However, their metabolic properties have barely been investigated. TSA is rapidly inactivated in rodents both in vitro and in vivo. We previously found that 5-(4-dimethylaminobenzoyl)aminovaleric acid hydroxyamide or 4-Me2N-BAVAH (compound 1) is metabolically more stable upon incubation with rat hepatocyte suspensions. In this study, we show that human hepatocytes also metabolize TSA more rapidly than compound 1 and that similar pathways are involved. Furthermore, structural analogs of compound 1 (compounds 2-9) are reported to have the same favorable metabolic properties. Removal of the dimethylamino substituent of compound 1 creates a very stable but 50% less potent inhibitor. Chain lengthening (4 to 5 carbon spacer) slightly improves both potency and metabolic stability, favoring HA reduction to hydrolysis. On the other hand, Cα-unsaturation and spacer methylation not only reduce HDAC inhibition but also increase the rate of metabolic inactivation approximately 2-fold, mainly through HA reduction. However, in rat hepatocyte monolayer cultures, compound 1 is shown to be extensively metabolized by phase II conjugation. In conclusion, this study suggests that simple structural modifications of amide-linked TSA analogs can improve their phase I metabolic stability in both rat and human hepatocyte suspensions. Phase II glucuronidation, however, can compensate for their lower phase I metabolism in rat hepatocyte monolayers and could play a yet unidentified role in the determination of their in vivo clearance. Copyright

Unique oxidation reaction of amides with pyridine-N-oxide catalyzed by ruthenium porphyrin: Direct oxidative conversion of N-acyl-L-proline to N-acyl-L-glutamate

Oxidations of alkanes, alkenes, and aromatic rings with pyridine N-oxides are efficiently catalyzed by ruthenium porphyrins under mild conditions. We show here that the oxidation of N-acyl cyclic amines with RuIVtetraarylporphyrin dichloride-2,6-substituted pyridine N-oxides directly gives N-acyl amino acids in modest to good yield via oxidative C-N bond cleavage. N-Acylpyrrolidines and N-acylpiperidines were converted to N-acyl-γ-aminobutyric acids and N-acyl-δ-aminovaleric acids, respectively. This type of reaction is a novel one in which the C-N bond is cleaved selectively at the less substituted carbon. Notably, the proline residue in proline-containing peptides was selectively converted to glutamate. A large intramolecular kinetic isotope effect (kH/kD = 9.8) was observed in the oxidation of N-benzoyl[2,2,-d2]pyrrolidine, indicating that the reaction should involve an α-hydrogen atom abstraction process as the rate-determining step. N-Acylcarbaldehyde, the putative intermediate ring-opened form of α-hydroxylated N-acyl cyclic amine, was readily oxidized with the oxidizing system to afford the corresponding N-acylamino acid in good yield. Further, lactams (1-methyl-2-pyrrolidone and 1-methyl- 2-piperidone) were also oxidized to give the corresponding imides (1-methylsuccinimide and 1-methylpiperidine-2,6-dione). Copyright

A Mechanism for bitter Taste Sensibility in Peptides

To estimate the steric distance between the bitter taste determinant sites in peptides, some cyclic dipeptides, amino acid anilides, amino acid cyclohexylamides, and benzoyl amino acids were synthesized and their tastes were evaluated.The diketopiperazine ring of cyclic dipeptides acted as a bitter taste determinant site due to its hydrophobicity.The steric distance between 2 sites was estimated as 4.1 Angstroem from the molecule models of cyclic dipeptides composed of typical amino acids in the bitter peptides.Due to the hypothesis of two bitter taste determinant sites, which bind with the bitter taste receptor via a "binding unit" and a "stimulating unit," a mechanism for the bitterness in peptides was postulated.

Composition containing a penem or carbapenem antibiotic and the use of the same

Administration of an N-acylated amino acid in association with a penem or carbapenem antibiotic relieves or eliminates the renal problems associated with administration of the antibiotic alone. The amino acid derivative and antibiotic may be formulated together as a composition or administered separately, either simultaneously or sequentially.

Composition containing a penem or carbapenem antibiotic

Administration of an N-acylated amino acid in association with a penem or carbapenem antibiotic relieves or eliminates the renal problems associated with administration of the antibiotic alone. The amino acid derivative and antibiotic may be formulated together as a composition or administered separately, either simultaneously or sequentially. The composition may be prepared by simple mixing.

KINETICS AND MECHANISM OF ACID HYDROLYSIS OF N-BENZOYL-L-LYSINES

Minor differences in acid hydrolysis rates of α- and ε-amide bonds in corresponding N-benzoyl-L-lysines have been found.The reaction is accelerated in the presence of free carboxyl group in the lysine-derivative molecule.The acid dissociation constants KAH of N - and Nε-benzoyl-L-lysines have been determined.Also the substituent effect in benzoyl group on the reaction rate has been examined.A mechanism of the acid hydrolysis of acyl derivatives of lysine is proposed.