2481-10-9

Usage

Uses

Used in Pharmaceutical Research:
D-S-tert-Butylcysteine is used as a research compound for its potential antioxidant and cytoprotective properties, making it a candidate for the development of treatments targeting neurodegenerative diseases and oxidative stress-related disorders.
Used in Chemical Synthesis:
Given its unique structure, D-S-tert-Butylcysteine is used as a building block in the synthesis of other complex organic compounds, particularly in the pharmaceutical and chemical industries, where its modified properties can be leveraged to create novel therapeutic agents or chemical intermediates.
Used in Antioxidant Formulations:
D-S-tert-Butylcysteine is used as an antioxidant in formulations designed to protect cells from oxidative damage, which is crucial in the prevention and treatment of a range of conditions associated with oxidative stress.
Used in Biochemical Studies:
In the field of biochemistry, D-S-tert-Butylcysteine is used as a tool to study the role of sulfur-containing amino acids in biological systems, providing insights into their function and potential therapeutic applications.
Each of these uses highlights the versatility and potential of D-S-tert-Butylcysteine in different industries, from pharmaceuticals to chemical synthesis, underpinning its importance in ongoing research and development efforts.

Upstream product

• 45157-84-4 S-t-butyl-L-cysteine t-butyl ester 
• 75-66-1 2-methylpropan-2-thiol 
• 52-90-4 L-Cysteine 
• 75-65-0 tert-butyl alcohol 
• 2481-11-0 S-tert-Butyl-L-cysteine tert-Butyl Ester Hydrochloride 
• 52-89-1 l-cysteine hydrochloride 

Downstream Products

• 56-89-3 L-cystine 
• 56976-06-8 N-(Carbo-tert-butoxy)-S-tert-butyl-L-cysteine 
• 75-66-1 2-methylpropan-2-thiol 
• 127-17-3 2-oxo-propionic acid 
• 109481-48-3 Z-Phe-Thr-Ser-Cys(t-Bu)-OH 

Relevant academic research and scientific papers

Cysteine-based fluorescence "turn-on" sensors for Cu2+and Ag+

We designed and synthesized twometal ion binding molecules 3a and 3b based on cysteine. In 3a, pyrene is used as a fluorescent probe, while 3b contains tryptophan, which acts as a fluorescent probe as well as facilitates metal ion binding. Detailed spectroscopic, calorimetric, microscopic and computational studies revealed the binding mode and the plausible structures of the complexes.

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%.

Asymmetric synthesis of β-lactams by intramolecular conjugate addition of serine and cysteine derivatives via memory of chirality

– The 4-exo-trig cyclization of axially chiral enolates generated from L-serine and L-cysteine dervatives proceeded predominately over β-elimination to give chiral β-lactams with contiguous tri- and tetrasubstituted carbon centers in up to 96% ee. The key to smooth production of β-lactams is the use of Cs2CO3and CF3CH2OH as a base and a proton source, respectively. A strongly electron-withdrawing Michael acceptor in the substrates was also critical for high enantioselectivity of the β-lactam formation.

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.