3262-64-4

Usage

Uses

Used in Pharmaceutical Industry:
(L)-3-(PROPARGYLSULFENYL)-ALANINE is used as a potential therapeutic agent for its anti-inflammatory, antioxidant, and anticancer properties. The presence of the propargylsulfenyl group allows it to modulate various biological pathways and exhibit inhibitory effects on inflammation, oxidative stress, and tumor growth, making it a candidate for the development of new drugs to treat related conditions.
Used in Research and Development:
(L)-3-(PROPARGYLSULFENYL)-ALANINE serves as a valuable compound in scientific research for exploring its potential applications in medicine. Its unique structure and biological activities provide a foundation for investigating its mechanisms of action, interactions with biological systems, and possible synergistic effects with other compounds, contributing to the advancement of medical knowledge and innovation.

InChI:InChI=1/C6H9NO2S/c1-2-3-10-4-5(7)6(8)9/h1,5H,3-4,7H2,(H,8,9)/t5-/m0/s1

Upstream product

• 52-90-4 L-Cysteine 
• 106-96-7 propargyl bromide 
• 52-89-1 l-cysteine hydrochloride 
• 624-65-7 2-propynyl chloride 
• 1262387-74-5 S-propargyl-N-[(1,1-dimethylethoxy)carbonyl]-L-cysteine methyl ester 

Downstream Products

• 3381-84-8 N-(2,4,6-Trinitro-phenyl)-S-2-propinyl-L-cystein 
• 1315318-67-2 (R)-4-(2,3-bis(tert-butoxycarbonyl)guanidino)butyl 4-((2-((tert-butoxycarbonyl)amino)-3-(prop-2-yn-1-ylthio)propanoyl)oxy)-3,5-dimethoxybenzoate 
• 3262-67-7 N-(2,4,6-Trinitro-phenyl)-S-1-propinyl-L-cystein 

Relevant academic research and scientific papers

New Tacrine Hybrids with Natural-Based Cysteine Derivatives as Multitargeted Drugs for Potential Treatment of Alzheimer's Disease

Alzheimer's disease (AD) is a devastating age-dependent neurodegenerative disorder. The main hallmarks are impairment of cholinergic system and accumulation in brain of beta-amyloid (Aβ) aggregates, which have been associated with oxidative damage and dyshomeostasis of redox-active biometals. The absence of an efficient treatment that could delay or cure AD has been attributed to the complexity and multifactorial nature of this disease. With this in mind and the recent interest on natural-based drugs, we have explored a set of natural-based hybrid compounds by conjugation of a tacrine moiety with an S-allylcysteine (garlic constituent) or S-propargylcysteine moiety aimed at improving the cholinergic system and neuroprotective capacity. The docking modeling studies allowed the selection of linkers to optimize the bimodal drug interaction with acetylcholinesterase enzyme (AChE) active site. The compounds were evaluated for some representative biological properties, including AChE activity and Aβ aggregation inhibition, as well as for their neuroprotective activity to Aβ- and ROS-induced cellular toxicity.

Leonurine derivative and application thereof in preparing medicine for preventing or treating ischemic cerebrovascular diseases

The invention provides a leonurine derivative and application of the leonurine derivative in preparation of a medicine for preventing or treating ischemic cerebrovascular diseases. The leonurine derivative has a structure as shown in a general formula (I), wherein X is selected from O or NH; Y is selected from any one of natural amino acid, substituted amino acid or amino alcohol; Z is selected from H, proline and any substituted proline. Pharmacological experiments prove that the leonurine derivative provided by the invention has the effects of neuroprotection, cerebral infarction area reduction and animal neurobehavioral scoring, and is good in safety, so that the leonurine derivative has important significance for developing novel medicines for preventing or treating ischemic cerebrovascular diseases.

Structure-activity relationship study and biological evaluation of SAC-Garlic acid conjugates as novel anti-inflammatory agents

A series of S-allyl-L-cysteine (SAC) with garlic acid conjugates as anti-inflammatory agents were designed and synthesized. Among the 40 tested compounds, SMU-8c exhibited the most potent inhibitory activity to Pam3CSK4-induced nitric oxide (NO) in RAW264.7 macrophages with IC50 of 22.54 ± 2.60 μM. The structure-activity relationship (SAR) study suggested that the esterified carboxyl group, carbon chain extension and methoxylation phenol hydroxy could improve the anti-inflammatory efficacy. Preliminary anti-inflammatory mechanism studies showed that SMU-8c significantly down-regulated the levels of Pam3CSK4 triggered TNF-α cytokine in human THP-1 cells, mouse RAW 264.7 macrophages, as well as in ex-vivo human peripheral blood mononuclear cells (PBMC) with no influence on cell viability. SMU-8c specifically blocked the Pam3CSK4 ignited secreted embryonic alkaline phosphatase (SEAP) signaling with no influence to Poly I:C or LPS triggered TLR3 or TLR4 signaling. Moreover, SMU-8c suppressed TLR2 in HEK-Blue hTLR2 cells and inhibited the formation of TLR1-TLR2, and TLR2-TLR6 complex in human PBMC. In summary, SMU-8c inhibited the TLR2 signaling pathway to down-regulate the inflammation cytokines, such as NO, SEAP and TNF-α, to realize its anti-inflammatory activity.

Derivative of Kutkin dimer analog JJA-D0 or its pharmaceutically acceptable salt, preparation method and use thereof

The invention relates to a derivative of Kutkin dimer analog JJA-D0 or its pharmaceutically acceptable salt, a preparation method and use thereof. The compound has a structure shown as a general formula (I). According to the invention, an alkyl group, an aryl group, a heteroaryl group, an alkoxycarbonylalkyl group, an acyl group, a sulfonate group, an antioxidant group such as a lipoic acid group,a H2S donor group such as a cysteine group, and a NO donor group such as a nitrate group are introduced to JJA-D0, and a series of structurally novel compounds can be synthesized and disclosed. The compounds inhibit NADPH oxidase and have superior anti-oxidation and anti-inflammatory pharmacological mechanisms by comparing with Kutkin, the compounds also have donor groups that provide NO and H2S,can further enhance pharmacological activity, and can be a new class of multifunctional compounds. The disclosed JJA-D0 derivative can be used for preparing health products or drugs for prevention ortreatment of diseases associated with NADPH oxidase, diseases associated with free radicals, diseases associated with inflammation, diseases associated with NO, and diseases associated with H2S.

Synthesis and conformational behavior of metallacyclicdipeptides derived from coordination of side chain alkynylamino acids to tungsten

Three dipeptides bearing alkynes on their side chains (9 (derived from dilysine), 14 (derived from dicysteine) and 17 (derived from diglycine)) were prepared and reacted with W(CO)3(dmtc)2 [dmtc = dimethyldithiocarbamate] to afford, respectively, three metallacyclicpeptides, 18, 19 and 20. The metallacyclicpeptides were characterized by HPLC, ES-MS, and 1H NMR. The conformational behavior of the alkynes about the tungsten center was assessed using 1H NMR. It was found that all three metallacyclicpeptides adopt multiple conformations of the alkynes relative to the tungsten. Both 18 and 19 appear to adopt all 8 possible conformations, while 20 adopts a limited number of conformations. The ability of the alkynes to equilibrate between the syn and anti conformations was assessed by examining the alkyne hydrogen resonances using variable temperature 1H NMR. It was found that the alkyne ligands in 18 and 19 will equilibrate between the syn and anti conformations. The alkyne hydrogen resonances in 18 coalesce to one signal around 343 K, while the alkyne hydrogen resonances in 19 do not completely coalesce even by 360 K. Complex 18 has a larger ring than complex 19, and the higher temperature of coalescence for 19 is attributed to its smaller ring size. In contrast, complex 20, which has the smallest ring size, cannot equilibrate between the syn and anti conformations, even at elevated temperatures. The results show that cyclic tungsten-bis(alkyne) complexes will form ring systems with ring sizes of approximately 10 atoms, that ring sizes of approximately 10 atoms are rigid, and that rigidity is lost as the ring size is increased.

Neoglycopeptides through direct functionalization of cysteine

Neoglycopeptides are readily prepared by direct functionalization of cysteine-containing peptides followed by click triazole formation between the resulting propargylated peptides and protected or free (2-azido)-ethyl gluco-, manno,- and galactopyranosides.

USE OF ALLYLCYSTEINE OR ITS ANALOGS AND PHARMACEUTICAL COMPOSITION THREROF

The invention discloses a use of compound S-allyl cysteine or its analogues in preparation of medicaments for preventing or treating myocardial injury and a preparation method thereof, as well as a pharmaceutical composition comprising the compound.

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.

Specificity of lysine: N6-hydroxylase: A hypothesis for a reactive substrate intermediate in the catalytic mechanism

The recombinant cytoplasmic preparation of lysine: N6-hydroxylase catalyzes the conversion of L-lysine to its N6-hydroxy derivative when supplemented with the cofactors NADPH and FAD. A number of lysine analogs reflecting minor alterations in the inherent structural features of the amino acid as well compounds with relatively high affinity for lysine binding domains in other proteins were examined for their ability to serve as substrates of lysine: N6-hydroxylase. These studies have revealed that the enzyme does not tolerate any change in the structural features of L-lysine, its preferred substrate, with the exception of the replacement of the C(γ)H2-methylene group by sulfur, as in (S)-2-aminoethyl-L-cysteine. L-Norleucine is a potent inhibitor of the enzyme while L-norvaline and L-α-aminobutyric acid do not exhibit such effect, indicating the importance of a C4 hydrophobic side chain for effective interaction with the enzyme. Among the N-alkyl amides of hydrophobic amino acids, only L-norleucine methylamide and L-α-aminobutyric acid ethylamide serve as moderate inhibitors of lysine: N6-hydroxylase. Based on the enzyme's stringent substrate specificity, a mechanism involving the conversion of L-lysine to 2-aminocaprolactam prior to its oxygenation by the 4α-peroxyflavin intermediate in the catalytic cycle is proposed.