23234-80-2

Usage

Uses

Used in Chemical Biology:
N-acetylpropargylglycine is used as a selective inhibitor for the enzyme 1-aminocyclopropane-1-carboxylic acid synthase, for its role in the biosynthesis of ethylene, which is essential in regulating the ripening and senescence of fruits and flowers.
Used in Anti-Aging Research:
N-acetylpropargylglycine is used as an anti-aging compound, as it has demonstrated the ability to extend the lifespan of certain organisms, such as the fruit fly Drosophila melanogaster, indicating its potential in the field of aging and longevity research.
Used in Neuroprotection:
N-acetylpropargylglycine is used in the study of neurodegenerative diseases, with its potential to protect against such conditions by reducing the production of toxic amyloid beta peptides in the brain, thereby offering a possible therapeutic approach for neurodegenerative disorders.
Used in Agricultural Applications:
In the agricultural industry, N-acetylpropargylglycine is used to manage the ripening process of fruits and flowers, potentially leading to extended shelf life and improved quality of produce.
Used in Medical Research:
In the medical field, N-acetylpropargylglycine is being investigated for its potential applications in treating neurodegenerative diseases and as a compound that could contribute to anti-aging therapies, offering new avenues for treatment and prevention strategies.

InChI:InChI=1/C7H9NO3/c1-3-4-6(7(10)11)8-5(2)9/h1,6H,4H2,2H3,(H,8,9)(H,10,11)

Upstream product

• 61172-60-9 diethyl α-acetamido-α-propargylmalonate 
• 50428-03-0 D,L-propargylglycine 
• 108-24-7 acetic anhydride 
• 61172-61-0 2-Acetylamino-2-prop-2-ynyl-malonic acid monoethyl ester 
• 106-96-7 propargyl bromide 
• 1068-90-2 2-acetylaminomalonic acid diethyl ester 
• 23235-05-4 L,D-acetylpropargylglycine ethyl ester 

Downstream Products

• 23235-01-0 (2S)-2-amino-4-pentynoic acid 
• 23235-01-0 (R)-2-aminopent-4-ynoic acid 
• 71460-15-6 tert-butyl D-propargylglycinate 
• 71460-15-6 2-amino-pent-4-ynoic acid tert-butyl ester 
• 1374442-49-5 C₁₉H₂₃IN₂O₄ 
• 1374442-50-8 C₁₉H₂₃IN₂O₄ 
• 1374442-51-9 C₁₉H₂₄N₂O₄ 
• 1374442-52-0 C₁₉H₂₄N₂O₄ 
• 1374442-46-2 C₁₇H₂₀N₂O₄ 
• 1374442-45-1 C₁₇H₂₀N₂O₄ 
• 1374442-44-0 C₁₇H₁₉IN₂O₄ 

Relevant academic research and scientific papers

Thrombin inhibitors based on a propargylglycine template

A series of novel arylsulfonylpropargylglycinamide derivatives was investigated as thrombin inhibitors in which the SAR was focused on substituents at the acetylchic terminus. Several compounds in this series were identified as potent thrombin inhibitors (Ki up to 5 nM) that are highly selective over trypsin and other serine proteases as well.

DL-propargyl glycine intermediate and preparation method thereof, and propargyl glycine preparation method based on intermediate

The invention relates to the field of amino acid preparation, in particular to a DL-propargyl glycine intermediate, a preparation method of the DL-propargyl glycine intermediate and a preparation method of propargyl glycine based on the DL-propargyl glycine intermediate. The preparation method of the DL-propargyl glycine intermediate comprises three steps of condensation, saponification and hydrolysis, and then corresponding derivatives can be obtained through a chemical resolution method and an enzyme resolution method respectively. According to the preparation method, the reaction time is shortened; the reaction is more thorough, thepreparation method of DL-propargyl glycine can be obtained through the reaction, two methods for preparing derivatives of D-propargyl glycine and L-propargylglycine are obtained at the same time, the prepared product is high in purity, secondary refining is not needed, the production cost is reduced, and industrial large-scale production is facilitated.

Gold-Catalyzed Cycloisomerization of Alkyne-Containing Amino Acids: Controlled Tuning of C–N vs. C–O Reactivity

Versatile alkyne-containing amino acids were used as ambident precursors in the divergent synthesis of alkylidenelactones and 1-pyrrolines. Two gold-catalyzed protocols were applied for selective intramolecular O- and N-cycloisomerization reactions.

Towards a biocompatible artificial lung: Covalent functionalization of poly(4-methylpent-1-ene) (TPX) with cRGD pentapeptide

Covalent multistep coating of poly(methylpentene), the membrane material in lung ventilators, by using a copper-free "click" approach with a modified cyclic RGD peptide, leads to a highly biocompatible poly(methylpentene) surface. The resulting modified membrane preserves the required excellent gas-flow properties while being densely seeded with lung endothelial cells.

Synthesis of modified phenylalanine peptides by cross enyne metathesis and a diels-alder reaction as key steps

Modified phenylalanine-based di- and tripeptides have been efficiently assembled by cross enyne metathesis and a Diels-Alder reaction as key steps under mild conditions. In all cases, peptide integrity was preserved, no racemisation was observed, and good yields of modified peptides were obtained.

Synthesis of ω-(hetero)arylalkynylated α-amino acid by sonogashira-type reactions in aqueous media

(Chemical Equation Presented) Mild conditions are described that allow the palladium-catalyzed cross-coupling of Cα-alkynylated glycine with a wide variety of electron-rich and electron-poor aryl and heteroaryl halides in aqueous media.

Elaboration of the side-chain of amino acid derivatives by palladium catalysed couplings

The palladium-catalysed couplings of aryl halides and triflates with propargyl amino amides and the couplings of aryl and vinyl halides and triflates with an ethynyl oxazolidine are reported.

NEW PENICILLINS FROM ISOPENICILLIN N SYNTHASE.

The three tripeptides δ-L-α-aminoadipoyl-L-cysteinyl-D-propargylglycine, δ-L-α-aminoadipoyl-L-cysteinyl-D-cyanoalanine and δ-L-α-aminoadipoyl-L-cysteinyl-D--norvaline were synthesised and incubated with the enzyme Isopenicillin N Synthase (IPNS).All incubation mixtures contained biologically active products, and led to the isolation of four new penicillins (β-ethyl, α-acetylenic, α- and β-nitrile) following purification by reverse phase HPLC.The stereochemistries of formation of monosubstituted penicillins with IPNS are rationalised.

Chloroanalyland propargylglycyl dipeptides. Suicide substrate containing antibacterials

A set of dipeptides containing the amino acid residues β-chloroalanine and propargylglycine, which are mechanism-based inactivators of purified microbial enzymes (alanine racemase and cystathionine γ-synthase, respectively), have been synthesized, and their antibacterial properties in vitro have been evaluated. Dipeptides containing a single β-chloro-L-alanyl residue (e.g., 3, 5, 9, and 10) or a single L-propargylglycyl residue (e.g., 12 and 15) are potent antibacterials. The in vitro antibiotic activity of β-chloro-L-alanine and of L-propargylglycine is increased as much as 4000-fold by incorporation of these residues into a dipeptide. Compounds that contain only a single enzyme-inactivating amino acid together with a second L-alanyl residue (3, 5, 12, and 15) have a restricted range of activity: of the species tested, only Streptococcus agalactiae, Staphylococcus aureus, and Staphylococcus epidermidis are sensitive. However, peptides that contain two suicide-substrate residues [e.g., β-Cl-LAla-β-Cl-LAla (8) or LppGly-LppGly (18)] are broad-spectrum antibacterials; as many as 12 different species of the 16 surveyed are sensitive. Dipeptides that contain an amino-terminal L-methionyl (9) or an L-norvalyl (10) residue and a carboxy-terminal β-chloro-L-alanyl unit are also effective against a large number of organisms; the spectra of activity are like those seen for 8 and 18. A 'mixed' dipeptide [β-Cl-LAla-LppGly, (21)] gives apparent synergism of antibiotic action of β-chloro-L-alanine and of L-propargylglycine when these two residues are incorporated into a single structure. Peptides of the D,D configuration (4, 6, 13, 16, and 20) and ones of L,D stereochemistry (e.g., 7) are not antibacterials. Peptides containing one (11 and 14) and two (17) D,L-propargylglycyl residues are unresolved sets of diastereomers; the mixtures of compounds are between two- and fourfold less active than the corresponding resolved L,L dipeptides (12, 15, and 18). These findings are consistent with a mechanism of action for these antibiotics involving stereoselective processing of the peptidyl unit in vivo.