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Nα-Benzoyl-L-arginine ethyl ester hydrochloride

Name: Nα-Benzoyl-L-arginine ethyl ester hydrochloride
Brand: BOC Sciences
Rating: 5 (1 reviews)

* Please kindly note that our products are not to be used for therapeutic purposes and cannot be sold to patients.

Category

L-Amino Acids

Catalog number

BAT-004099

CAS number

2645-08-1

Molecular Formula

C15H22N4O3·HCl

Molecular Weight

342.80

Nα-Benzoyl-L-arginine ethyl ester hydrochloride

IUPAC Name

ethyl (2S)-2-benzamido-5-(diaminomethylideneamino)pentanoate;hydrochloride

Synonyms

Bz-L-Arg-OEt HCl; BZ-ARGININE-OET HCl; HCl N-benzoyl-L-arg-OEt; Bz-Arg-Oet HCl; BENZOYL-ARG-OET HCl; Nalpha-Benzoyl-L-arginine ethyl ester hydrochloride

Appearance

White to off-white powder

Purity

≥ 99% (HPLC)

Density

1.23 g/cm3

Melting Point

128-135 °C

Storage

Store at 2-8 °C

InChI

InChI=1S/C15H22N4O3.ClH/c1-2-22-14(21)12(9-6-10-18-15(16)17)19-13(20)11-7-4-3-5-8-11;/h3-5,7-8,12H,2,6,9-10H2,1H3,(H,19,20)(H4,16,17,18);1H/t12-;/m0./s1

InChI Key

HIXDELXKSSLIKB-YDALLXLXSA-N

Canonical SMILES

CCOC(=O)C(CCCN=C(N)N)NC(=O)C1=CC=CC=C1.Cl

Nα-Benzoyl-L-arginine ethyl ester hydrochloride is a synthetic derivative widely used in biochemical and pharmacological research. Here are some key applications of Nα-Benzoyl-L-arginine ethyl ester hydrochloride:

Enzyme Assays: This compound is commonly used as a substrate in enzyme assays to study the activity of proteases like trypsin. By monitoring the hydrolysis of Nα-Benzoyl-L-arginine ethyl ester hydrochloride, researchers can quantitatively measure enzyme kinetics. This application is crucial in understanding enzyme behavior and in the development of enzyme inhibitors.

Drug Development: In the pharmaceutical industry, Nα-Benzoyl-L-arginine ethyl ester hydrochloride is used for screening potential inhibitory compounds against proteases. By serving as a model substrate, it helps in elucidating the inhibitory mechanisms of novel drug candidates. This is particularly important in the development of therapeutic agents for diseases involving protease dysregulation.

Protein Structure Studies: Researchers use Nα-Benzoyl-L-arginine ethyl ester hydrochloride to investigate the structural properties and active sites of proteases. By observing how various proteases interact with this compound, valuable information can be gained regarding substrate specificity and enzyme-substrate interactions. These insights facilitate the rational design of enzyme mutants with desired characteristics.

Biotechnology: In biotechnological applications, Nα-Benzoyl-L-arginine ethyl ester hydrochloride can be used to refine the production processes of recombinant proteases. By optimizing the conditions for enzyme activity and stability using this compound, production yields can be enhanced. This is essential for industrial applications of proteases in areas like detergents, food processing, and medical diagnostics.

1. Identification of serine proteases from Leishmania braziliensis

Herbert L M Guedes, João M Neto Rezende, Mayra A Fonseca, Cristiane M C Salles, Bartira Rossi-Bergmann, Salvatore Giovanni De-Simone Z Naturforsch C J Biosci. 2007 May-Jun;62(5-6):373-81. doi: 10.1515/znc-2007-5-610.

Leishmania (V) braziliensis is one of the most important ethiologic agents of the two distinct forms of American tegumentary leishmaniasis (cutaneous and mucosal). The drugs of choice used in leishmaniasis therapy are significantly toxic, expensive and are associated with frequent refractory infections. Among the promising new targets for anti-protozoan chemotherapy are the proteases. In this study, serine proteases were partially purified from aqueous, detergent and extracellular extracts of Leishmania braziliensis promastigotes by aprotinin-agarose affinity chromatography. By zymography, the enzymes purified from the aqueous extract showed apparent activity bands of 60 kDa and 45 kDa; of 130 kDa, 83 kDa, 74 kDa and 30 kDa from the detergent extract; and of 62 kDa, 59 kDa, 57 kDa, 49 kDa and 35 kDa from the extracellular extract. All purified proteases exhibited esterase activity against Nalpha-benzoyl-L-arginine ethyl ester hydrochloride and Nalpha-p-tosyl-L-arginine methyl ester hydrochloride (serine protease substrates) and optimal activity at pH 8. 0. Proteases purified from the aqueous and extracellular extracts were effectively inhibited by benzamidine (trypsin inhibitor) and those from the detergent extract were inhibited by N-tosyl-L-phenyl-alanine chloromethyl ketone (chymotrypsin inhibitor) indicating that all these enzymes are serine proteases. These findings indicate that L. braziliensis serine proteases display some biochemical similarities with L. amazonensis serine proteases, demonstrating a conservation of this enzymatic class in the Leishmania genus. This is the first study to report the purification of a serine protease from Leishmania braziliensis.

2. Identification of serine protease as a major allergen of Curvularia lunata

R Gupta, V Sharma, S Sridhara, B P Singh, N Arora Allergy. 2004 Apr;59(4):421-7. doi: 10.1046/j.1398-9995.2003.00378.x.

Background: Several proteins from Curvularia lunata have been identified as important fungal allergens. It will be worthwhile to study the functional aspects of these allergens. The present study aimed at purifying a major allergen and determining its biological function. Methods: Concanavalin A and Superdex 75 were used to purify Cur l 1 major allergen from C. lunata. Cur l 1 activity was determined qualitatively and quantitatively. Serine protease inhibitors and specific substrate was used to determine the biological function of the protein. Results: Concanavalin A-bound fraction showed five allergenic proteins, which on Superdex G-75 purification gave a homogenous Cur l 1 protein. Cur l 1 showed IgE reactivity with 80% of the C. lunata hypersensitive patient's sera indicating it to be a major allergen. It showed protease activity on different substrates. Cur l 1's amino terminal sequence, GLTQKSAPWGLGADTIVAVELDSY, showed homology with the alkaline serine protease precursor. Phenylmethylsulfonylfluoride, pefabloc, aprotinin and leupeptin inhibited 70-80% enzymatic activity of Cur l 1 and no inhibition was observed with ethylenediaminetetraacetic acid (EDTA). A dose-dependent hydrolysis of Nalpha-benzoyl-l-arginine ethyl ester-hydrochloride, a specific serine protease substrate was obtained with Cur l 1. Conclusion: A major glycoprotein allergen Cur l 1 was purified to homogeneity from C. lunata. Amino terminal sequence and biochemical assays identified it as a serine protease.