4134-56-9

Usage

Uses

Used in Pharmaceutical Development:
S-Butyl-D-cysteine is used as a building block for the synthesis of biologically active compounds, leveraging its distinct structural properties to create novel pharmaceutical agents.
Used in Antioxidant Research:
S-Butyl-D-cysteine is studied for its potential role in human health, particularly concerning its impact on oxidative stress and antioxidant activity, which may contribute to the understanding of its therapeutic benefits.
Used in Drug Design:
In the field of medicinal chemistry, S-Butyl-D-cysteine is utilized as a key component in the design of new drugs, potentially leading to advancements in treatment options for various diseases and conditions.

InChI:InChI=1/C7H15NO2S/c1-3-5(2)8-6(4-11)7(9)10/h5-6,8,11H,3-4H2,1-2H3,(H,9,10)/t5?,6-/m0/s1

Upstream product

• 109-65-9 1-bromo-butane 
• 52-90-4 L-Cysteine 
• 109-69-3 n-Butyl chloride 
• 52-89-1 l-cysteine hydrochloride 
• 19216-62-7 S-n-Butyl-N-acetyl-L-cysteine 
• 109-79-5 n-butanethiol 
• 542-69-8 1-iodo-butane 
• 67194-09-6 Boc-Cys(Buⁿ) 

Downstream Products

• 20702-80-1 (+)S-butyl-L-cysteine sulfoxide 
• 19216-62-7 S-n-Butyl-N-acetyl-L-cysteine 
• 110949-51-4 (R)-2-(2-Benzoylsulfanylmethyl-3-phenyl-propionylamino)-3-butylsulfanyl-propionic acid 
• 110949-60-5 (R)-3-Butylsulfanyl-2-(2-mercaptomethyl-3-phenyl-propionylamino)-propionic acid 

Relevant academic research and scientific papers

Subtype-Specific Agonists for NMDA Receptor Glycine Binding Sites

A series of analogues based on serine as lead structure were designed, and their agonist activities were evaluated at recombinant NMDA receptor subtypes (GluN1/2A-D) using two-electrode voltage-clamp (TEVC) electrophysiology. Pronounced variation in subunit-selectivity, potency, and agonist efficacy was observed in a manner that was dependent on the GluN2 subunit in the NMDA receptor. In particular, compounds 15a and 16a are potent GluN2C-specific superagonists at the GluN1 subunit with agonist efficacies of 398% and 308% compared to glycine. This study demonstrates that subunit-selectivity among glycine site NMDA receptor agonists can be achieved and suggests that glycine-site agonists can be developed as pharmacological tool compounds to study GluN2C-specific effects in NMDA receptor-mediated neurotransmission.

Efficient S-alkylation of cysteine in the presence of 1,1,3,3- tetramethylguanidine

The synthesis of S-alkylated cysteine derivatives was carried out successfully in the presence of 1,1,3,3-tetramethylguanidine. Alkylation proceeded in high yields on unprotected amino acids and peptides containing a sulfhydryl group.

Method Of Synthesizing S-Allyl-Cysteine Analogues And Their Therapeutic Application In Treating Myocardial Infarction

A pharmaceutical composition and methods of producing and application of the composition for treating myocardial infarction of a subject are disclosed. The pharmaceutical composition comprises a therapeutically effective amount of at least one synthesized compound selected from the group consisting of SEC, SPC, SBC, SPEC, SAC, SAMC, and SPRC, and a pharmaceutically acceptable carrier.

ALPHA-HELICAL MIMETICS

Benzoyl urea derivatives that are alpha helical peptide mimetics that mimic BH3-only proteins, compositions containing them, their conjugation to cell-targeting moieties, and their use in the regulation of cell death are disclosed. The benzoyl urea derivatives are capable of binding to and neutralising pro-survival Bcl-2 proteins. Use of the benzoyl urea derivatives in the treatment and/or prophylaxis of diseases or conditions associated with deregulation of cell death are also disclosed.

Asymmetric synthesis of S-alkyl-substituted (R)-cysteines via a chiral NiII complex of the Schiff's base of dehydroalanine with (S)-2-N-(N-benzylprolyl)aminobenzophenone

An efficient procedure was developed for the asymmetric synthesis of S-alkyl derivatives of (R)-cysteine by nucleophilic addition of alkanethiols (BunSH, ButSH, or tert-C5H11SH) to the C=C bond of the dehydroalanine fragment in the Ni11 complex of the Schiff's base of Δ-Ala with (S)-2-N-(N-benzylprolyl)aminobenzophenone [(S)-BPB-Δ-Ala]Ni11. Under conditions of thermodynamic control of the reaction, the diastereomeric excess of the complexes with the (S,R)-configuration was 88 - 96%. After decomposition of the complexes, (R)-S-butylcysteine, (R)-S-tert-butylcysteine, and (R)-S-tert-pentylcysteine were isolated with an enantiomeric purity of >97%.

Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N- acetyl-L-cysteines

The aminoacylase that catalyzes the hydrolysis of N-acetyl-L-cysteine (NAC) was identified as acylase I after purification by column chromatography and electrophoretic analysis. Rat kidney cytosol was fractionated by ammonium sulfate precipitation, and the proteins were separated by ion-exchange column chromatography, gel-filtration column chromatography, and hydrophobic interaction column chromatography. Acylase activity with NAC and N-acetyl-L- methionine (NAM), a known substrate for acylase I, as substrates coeluted during all chromatographic steps. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the protein was purified to near homogeneity and had a subunit M(r) of 43 000, which is identical with the M(r) of acylase I from porcine kidney and bovine liver. n-Butylmalonic acid was a slow-binding inhibitor of acylase I and inhibited the deacetylation of NAC with a K(i) of 192 ± 27 μM. These results show that acylase I catalyzes the deacetylation of NAC. The acylase I-catalyzed deacetylation of a range of S-alkyl-N- acetyl-L-cysteines, their carbon and oxygen analogues, and the selenium analogue of NAM was also studied with porcine kidney acylase I. The specific activity of the acylase I-catalyzed deacetylation of these substrates was related to their calculated molar volumes and log P values. The S-alkyl-N- acetyl-L-cysteines with short (C0-C3) and unbranched S-alkyl substituents were good acylase I substrates, whereas the S-alkyl-N-acetyl-L-cysteines with long (>C3) and branched S-alkyl substituents were poor acylase I substrates. The carbon and oxygen analogues of S-methyl-N-acetyl-L-cysteine and the carbon analogue of S-ethyl-N-acetyl-L-cysteine were poor acylase I substrates, whereas the selenium analogue of NAM was a good acylase I substrate.