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Application Area

S-Benzyl-L-cysteine 7-amido-4-methylcoumarine

* 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-006065

CAS number

80173-27-9

Molecular Formula

C20H20N2O3S

Molecular Weight

368.45

S-Benzyl-L-cysteine 7-amido-4-methylcoumarine

IUPAC Name

(2S)-2-amino-3-benzylsulfanyl-N-(4-methyl-2-oxochromen-7-yl)propanamide

Synonyms

H-Cys(Bzl)-AMC

Purity

99%

Boiling Point

618.9±55.0 °C

Storage

Store at -20°C

InChI

InChI=1S/C20H20N2O3S/c1-13-9-19(23)25-18-10-15(7-8-16(13)18)22-20(24)17(21)12-26-11-14-5-3-2-4-6-14/h2-10,17H,11-12,21H2,1H3,(H,22,24)/t17-/m1/s1

InChI Key

WSBODWFAIQZWSU-QGZVFWFLSA-N

Canonical SMILES

CC1=CC(=O)OC2=C1C=CC(=C2)NC(=O)C(CSCC3=CC=CC=C3)N

S-Benzyl-L-cysteine 7-amido-4-methylcoumarine, a chemical compound with specific applications in biochemical and research settings, finds diverse utility in scientific endeavors.

Enzyme Activity Assays: Serving as a fluorescent substrate, S-Benzyl-L-cysteine 7-amido-4-methylcoumarine stands out as a pivotal tool for assessing the activity of specific enzymes. Upon enzymatic cleavage, the substrate liberates a fluorescent product, which can be quantified using a fluorometer. This method plays a crucial role in the high-throughput screening of enzyme inhibitors and activators in the realm of drug discovery, enabling the rapid identification of potential therapeutic agents.

Protease Research: As a herald in protease studies, this compound acts as a potent reporter molecule, shedding light on the intricate workings of enzymes that degrade proteins. By devising assays centered around S-Benzyl-L-cysteine 7-amido-4-methylcoumarine, researchers can delve into the intricacies of protease activity and specificity across different varieties. This investigative approach holds significance in unraveling the functional nuances of proteases in physiological processes and disease states, paving the way for advanced therapeutic interventions.

Diagnostic Tool Development: In the arena of diagnostic tool innovation, S-Benzyl-L-cysteine 7-amido-4-methylcoumarine emerges as a cornerstone for crafting assays that detect enzyme activity in clinical specimens. These diagnostic assays serve as potent tools for identifying conditions marked by irregular enzyme function, such as certain cancers or genetic anomalies. Featuring high sensitivity and specificity, these assays play a crucial role in early disease detection and monitoring disease progression, ultimately enhancing patient outcomes and treatment efficacy.

Molecular Biology Research: Within the realm of molecular biology, this compound finds multifaceted applications in fluorescence-based techniques aimed at exploring protein interactions and subcellular localization dynamics within living cells. When integrated with cutting-edge imaging modalities, S-Benzyl-L-cysteine 7-amido-4-methylcoumarine enables researchers to visualize dynamic molecular processes in real-time. This visual elucidation aids in unraveling the complexities of biological pathways and mechanisms, shedding light on fundamental biological processes at a granular level.

1. Synthesis of Glycyrrhizic Acid Conjugates with S-Benzyl-L-Cysteine and Their Antiviral Activity

L A Baltina, R M Kondratenko, L A Baltina Jr, O A Plyasunova Pharm Chem J. 2021;55(3):224-227. doi: 10.1007/s11094-021-02402-3. Epub 2021 Jun 14.

A new method for the synthesis of glycyrrhizic acid (GA) conjugates with S-benzyl-L-cysteine using 1-ethyl-3-(3-dimethylaminoproopyl)carbodiimide is proposed. It is established that 3-O-{2-O-[N-(β-D-glucopyranosyluronyl)-L-cysteine-S-benzyl]-N-(β-D-glucopyranosyluronyl)-L-cysteine-S-benzyl}-(3β,20β)-11-oxo-30-(N-carbonyl-L-cysteine-S-benzyl)-30-norolean-12-ene is superior to GA in inhibiting the accumulation of HIV-I virus-specific protein p24 (viral antigen) in MT-4 cell culture (IC50 3 μg/mL, SI 90) and is 50 - 55 times less toxic to cells than azidothymidine.

2. The effect of ε-aminocaproyl-S-benzyl-L-cysteine on the t-PA activity of human saliva

K Midura-Nowaczek, J Kaczyńska, I Bruzgo, A Markowska, D Drozdowska Adv Med Sci. 2011;56(2):323-6. doi: 10.2478/v10039-011-0039-6.

Purpose: The aim of this work was to study the effect of the synthetic antifibrinolytics: ε-aminocaproic acid (EACA), tranexamic acid (AMCHA) and ε-aminocaproyl-S-benzyl-L-cysteine (H-EACA-S-Bzl-L-Cys-OH) on the fibrinolytic activity of saliva in order to obtain new data on the activity of saliva tissue plasminogen activator (t-PA). Material and methods: Saliva samples were obtained from healthy volunteers. Saliva, precipitate and supernatant were tested 1hr, 4 hrs and 6hrs after collection. The effect of the synthetic antifibrinolytics was examined with the use of the clot lysis time determination. Results: All examined compounds inhibited the fibrinolytic activity of saliva 1hr after collection. H-EACA-S-Bzl-L-Cys-OH was the most active inhibitor. After 6 hours in room temperature only this compound showed a certain possibility to prolong the clot lysis time. Conclusions: The obtained results may indicate the possibility of the difference in specificity between the activities of t-PA of saliva and recombinant tissue plasminogen activator activities. It may explain the unexpected high inhibitory activity of H-EACA-S-Bzl-L-Cys-OH in our study.

3. Oxidation of cysteine S-conjugates by rabbit liver microsomes and cDNA-expressed flavin-containing mono-oxygenases: studies with S-(1,2-dichlorovinyl)-L-cysteine, S-(1,2,2-trichlorovinyl)-L-cysteine, S-allyl-L-cysteine, and S-benzyl-L-cysteine

S L Ripp, L H Overby, R M Philpot, A A Elfarra Mol Pharmacol. 1997 Mar;51(3):507-15.

Rabbit liver microsomes catalyzed the highly stereoselective, NADPH- and time-dependent S-oxidation of S-benzyl-L-cysteine (SBC), S-allyl-L-cysteine (SAC), S-(1,2-dichlorovinyl)-L-cysteine (DCVC), and S-(1,2,2-trichlorovinyl)-L-cysteine (TCVC) to their respective sulfoxides. Methimazole, a flavin-containing mono-oxygenase (FMO) substrate, inhibited S-oxidation of all four conjugates. The cytochrome P450 inhibitor 1-benzylimidazole did not affect SAC, SBC, or DCVC S-oxidation but inhibited the S-oxidation of TCVC. Solubilization of microsomes also inhibited TCVC activity, whereas SBC, SAC, and DCVC activities were not affected. Because these results suggested that FMOs were the major catalysts of SBC, SAC, and DCVC sulfoxidations, the four conjugates were evaluated as substrates for cDNA-expressed rabbit FMO isoforms FMO1, FMO2, FMO3, and FMO5. At equimolar concentrations (10 mM), FMO1 S-oxidized SBC and SAC, but no sulfoxides were detected with DCVC or TCVC. FMO3 S-oxidized all four conjugates. Km values determined with FMO3 were comparable to Km values from rabbit liver microsomes. S-Oxidation by FMO2 was detected only with SAC, and no sulfoxides were detected in incubations with FMO5. These results show that FMO isoforms can catalyze cysteine conjugate S-oxidation and that the specific isoform involved depends on the structure of the cysteine conjugate. The cysteine conjugates with more nucleophilic sulfur atoms, SAC and SBC, were much better FMO substrates than those having the less nucleophilic sulfur atoms DCVC and TCVC. The sulfoxides of TCVC and DCVC were reactive toward GSH, whereas the sulfoxides of SBC and SAC were not reactive. These results provide evidence for different chemical reactivities of these sulfoxides.