6453-58-3

Usage

Uses

Used in Pharmaceutical Industry:
5-[[AMINO(IMINO)METHYL]AMINO]-2-(BENZOYLAMINO)PENTANOIC ACID is used as a research compound for exploring its potential applications in drug development. Its unique structure and potential interactions with biological systems make it a promising candidate for the development of new pharmaceuticals.
Used in Drug Development:
5-[[AMINO(IMINO)METHYL]AMINO]-2-(BENZOYLAMINO)PENTANOIC ACID is used as a lead compound in the discovery and optimization of new drugs. Its chemical properties and potential biological activities can be further investigated to identify its therapeutic potential and develop it into a viable drug candidate.
Used in Amino Acid Derivative Research:
5-[[AMINO(IMINO)METHYL]AMINO]-2-(BENZOYLAMINO)PENTANOIC ACID is used as a model compound in the study of amino acid derivatives and their biological activities. Understanding the structure-activity relationships of 5-[[AMINO(IMINO)METHYL]AMINO]-2-(BENZOYLAMINO)PENTANOIC ACID can provide insights into the design and synthesis of novel amino acid-based drugs.
Used in Biological Activity Studies:
5-[[AMINO(IMINO)METHYL]AMINO]-2-(BENZOYLAMINO)PENTANOIC ACID is used as a test compound in biological assays to evaluate its interactions with biological systems. This can help identify its potential pharmacological properties and guide further research into its therapeutic applications.
Used in Medicinal Chemistry:
5-[[AMINO(IMINO)METHYL]AMINO]-2-(BENZOYLAMINO)PENTANOIC ACID is used as a starting material in the synthesis of novel compounds with potential medicinal properties. Its unique structure can be modified and optimized to develop new drugs with improved efficacy and selectivity.

Upstream product

• 420-04-2 CYANAMID 
• 4668-32-0 N^α-Benzoylornithine 
• 154-92-7 Nα-benzoyl-L-arginine 
• 911-76-2 N-α-benzoyl-DL-arginine-p-nitroanilide 
• 911-77-3 alpha-N-benzoyl-DL-arginine-p-nitroanilide hydrochloride 

Downstream Products

• 1784-04-9 N^α-benzoyl-L-arginine methyl ester hydrochloride 
• 7200-25-1 Arg 

Relevant academic research and scientific papers

Microwave radiation accelerates trypsin-catalyzed peptide hydrolysis at constant bulk temperature

The influence of microwave radiation on trypsin activity was explored using a CEM CoolMate apparatus at a constant bulk temperature. Digestion of Nα(±)-benzoyl-d/l-arginine-4-nitroanilide hydrochloride, azocasein and casein catalyzed by trypsin from the b

Sodium periodate oxidized cotton yarn as carrier for immobilization of trypsin

Cotton yarn was first oxidized by sodium periodate to introduce aldehyde groups which were able to react with amino groups of trypsin to form Schiff's base, and result in cotton yarn immobilized trypsin. The effect of periodate oxidation on the chemical a

Hybrid biofunctional nanostructures as stimuli-responsive catalytic systems

A novel active biocatalytic reaction system is proposed by covalently immobilizing porcine pancreas trypsin within the thermoresponsive polymer shell of superparamagnetic Fe3O4 nanoparticles. Active ester-functional nanocarriers suit

A continuous bioreactor prepared via the immobilization of trypsin on aldehyde-functionalized, ring-opening metathesis polymerization-derived monoliths

The ring-opening metathesis polymerization (ROMP) of norborn-2-ene (NBE) and cis-cyclo- octene (COE) was initiated with well-defined Grubbs-type initiators, i.e., RuCl2(CHPh)(PCy3)2 (1), [RuCl2(PCy3)- (IMesH2)(CHPh)] (2), and [RuCl2(3-Br-Py)2(IMesH2)(CHPh)] (3)(MesH 2 = 1, 3-bis(2, 4, 6-trimethylphenyl)- imidazolin-2-ylidene, PCy 3 = tricyclohexylphosphine, 3-Br-Py = 3-bromopyridine). Reaction of the living polymers with O2 (air) resulted in the formation of aldehyde-semitelechelic polymers in up to 80% yield, depending on the initiator and monomer used. To proof aldehyde formation, the terminal aldehyde groups were converted into the corresponding 2, 4-dinitrophenylhydrazine derivatives, and the structure of the hydrazones was confirmed by NMR and IR spectroscopy. This simple methodology was then used for the functionalization of ROMP-derived monoliths prepared from NBE, 1, 4, 4a, 5, 8, 8a-hexahydro-1, 4, 5, 8-exo-endo-dimethanonaphthalene (DMN-H6) and (NBE-CH2O) 3SiCH3, to yield aldehyde-funtionalized monoliths. The extent of aldehyde formation was determined by hydrazone formation. Up to 8 μmol of aldehyde groups/g monolith could be generated by this approach. Finally, these aldehyde-functionalized monoliths were used for the immobilization of trypsin. Excellent proteolytic activity of the immobilized enzyme was found both under batch and continuous flow conditions.

Photoregulation of the activities of proteins

Azobenzene modified papain, reveals photoregulation toward hydrolysis of Nα-benzoyl-DL-arginine-4-nitroanilide. The association constants of thiophenefulgide modified concanavolin A (Con. A) towards monosaccharides is reversibly photoregulated. Immobilize

Oxidation of Dithiols by Flavopapain

The redox reactions between flavopapain 1 and various dithiols have been examined under anaerobic conditions.The semisynthetic enzyme is an effective catalyst relative to the model flavin, 7-acetyl-10-methylisoalloxazine (3).Relative rate enhancements, (kcat/Km)/k2model, observed are 3.9, 8.0, and 17.4 for dithiotreitol, d,l-dihydrolipoic acid, and d,l-dihydrolipoamide, respectively.This substrate specificity, also seen in N-alkyl-1,4-dihydronicotinamide series, is explicable in terms of favorable hydrophobic-hydrophobic binding interaction between the substrates and the enzyme active site.Stereospecificity was not observed in the enzymatic reactions of the dithiols.It is demonstrated that the enzyme and model flavin reactions of the dithiols both proceeded via comparable mechanistic pathway.