598-41-4

Usage

Definition

ChEBI:Glycinamide is an amino acid amide and a glycine derivative.

Synthesis

The mild and effective aminodibromination reaction of nitroolefins with amphoteric ions as organocatalysts resulted in the efficient conversion of aminodibromo products to glycinamide.

InChI:InChI=1/C2H6N2O/c3-1-2(4)5/h1,3H2,(H2,4,5)

Upstream product

• 1816-91-7 2-azido-acetamide 
• 71990-03-9 iodo-acetic acid-(hydroxymethyl-amide) 
• 56-40-6 glycine 
• 459-73-4 GlyOEt*HCl 
• 79-07-2 Chloroacetamide 
• 114444-46-1 C₁₄H₁₃NO 
• 105-39-5 chloroacetic acid ethyl ester 
• 106827-72-9 Trt-L-Hse(Trt)-Gly-NH₂ 
• 76990-56-2 milacemide 
• 540-61-4 2-aminoacetonitrile 
• 623-73-4 diazoacetic acid ethyl ester 
• 7664-41-7 ammonia 
• 7732-18-5 water 
• 306-14-9 L-histidyl-L-histidine 

Downstream Products

• 4596-57-0 2-(((benzylthio)carbonothioyl)amino)acetic acid 
• 949-90-6 N-(carbobenzyloxy)glycinamide 
• 57229-36-4 2,3-Dimethyl-5-hydroxypyrazine 
• 859326-59-3 N-benzoylthiocarbamoyl-glycine amide 
• 18591-57-6 5,6-diphenyl-2-hydroxypyrazine 
• 18591-57-6 2,3-Diphenyl-6-hydroxypyrazine 
• 4238-57-7 2-formylaminoacetamide 
• 17187-05-2 Z-L-phenylalanylglycinamide 
• 2276-20-2 N-(N-benzyloxycarbonyl-DL-leucyl)-glycine amide 
• 145133-90-0 2-amino-N-(o-tolyl)acetamide 
• 98863-04-8 N-(N,N-phthaloyl-phenylalanyl)-glycin-amide 
• 103758-70-9 (+/-)-N-(threo-2,6-bis-benzyloxycarbonylamino-5-hydroxy-hexanoyl)-glycine amide 
• 54495-46-4 N-(2,6-Dinitro-4-trifluormethylphenyl)glycinamid 
• 62665-79-6 C₁₅H₁₄N₂O₂ 

Relevant academic research and scientific papers

Nickel(III) oxidation of its glycylglycylhistamine complex

The doubly-deprotonated Ni(III) complex of Gly2Ha (where Ha is histamine) undergoes base-assisted oxidative self-decomposition of the peptide. At ≤ p[H+] 7.0, a major pathway is a two-electron oxidation at the a-carbon of the N-terminal glycyl residue. Major products (up to 73%) of this two-electron oxidation are glyoxylglycylhistamine and ammonia. Glyoxylglycylhistamine will decay to give isocyanatoacetylhistamine and formaldehyde. Two-electron oxidations of the second glycyl and histamine residues occur as minor pathways (12% of the total possible reaction). Above p[H+] 8.5, two Ni(III)-peptide complexes form an oxo bridge in the axial positions to give a reactive dimer species. This proximity allows the resulting Ni(III)-peptide radical intermediates to undergo peptide-peptide cross-linking at the N-terminal glycyl residues. The products found below p[H+] 7.0 are observed above p[H+] 8.5 as well, although in lower yields. In contrast to this work, NiIII(H- 2Gly2HisGly) undergoes a four-electron oxidation at the N-terminal glycyl residue. Oxidation at the internal glycyl and histidyl residues are not observed. The reactivity of NiIII(H -2Gly2Ha)+ is also different than Cu III(H-2Gly2Ha)+, which undergoes a two-electron oxidation at the histamine group with no peptide-peptide cross-linking in basic solution.

Conformational preference of glycinamide in solution: An answer derived from combined experimental and computational studies

Conformational problems are often subtle but very important in controlling many intricate features in chemistry and biochemistry. We have performed the conformational analysis of glycinamide using NMR experiments and computational studies. 1H NMR experiments suggest the prevalence of intramolecular hydrogen bonded conformation of glycinamide (2B) in acetonitrile, whereas, non-intramolecular hydrogen bonded conformation 2A is favoured in dimethylsulfoxide. The NOESY experiments carried out for glycinamide in DMSO-d6, showed stronger NOE interaction of the NHa-atom of amide group with CH2 than that of NHb-atom confirming the presence of conformer 2A. DFT calculations performed with explicit DMSO molecules also suggested a clear preference for the conformer 2A. The molecular dynamics simulations performed with the explicit DMSO molecules also showed that the intermolecular hydrogen bonding exists between the solvent and solute molecules to stabilize the conformer 2A. The present study sheds light on the debate of conformational preference of neutral glycinamide in the present literature.

Preparation method of 2, 6-dichloropyrazine

The invention discloses a preparation method of 2, 6-dichloropyrazine. The method comprises the following steps: taking glycine and glyoxal as raw materials, carrying out ammoniation and cyclization reactions to prepare 2-hydroxypyrazine sodium; and reacting 2-hydroxypyrazine sodium with thionyl chloride under the catalytic action of N,N-diisopropylethylamine to prepare 2-chloropyrazine; wherein pyridine is used as a solvent, and 2-chloropyrazine is subjected to chlorination of chlorine to obtain 2,6-dichloropyrazine. The method has the advantages that the raw material namely glycine is cheapand easily available, and phosphorus oxychloride is not used as a chlorination reagent, so that the generation of organic phosphorus-containing wastewater is greatly reduced, and an effective way is provided for efficient green industrial production of 2, 6-dichloropyrazine.

Corresponding amine nitrile and method of manufacturing thereof

The invention relates to a manufacturing method of nitrile. Compared with the prior art, the manufacturing method has the characteristics of significantly reduced using amount of an ammonia source, low environmental pressure, low energy consumption, low production cost, high purity and yield of a nitrile product and the like, and nitrile with a more complex structure can be obtained. The invention also relates to a method for manufacturing corresponding amine from nitrile.

Tuning the reactivity of nitriles using Cu(ii) catalysis-potentially prebiotic activation of nucleotides

During the transition from prebiotic chemistry to biology, a period of solution-phase, non-enzymatic activation of (oligo)nucleotides must have occurred, and accordingly, a mechanism for phosphate activation must have existed. Herein, we detail results of an investigation into prebiotic phosphate activation chemistry using simple, prebiotically available nitriles whose reactivity is increased by Cu2+ ions. Furthermore, although Cu2+ ions are known to catalyse the hydrolysis of phosphodiester bonds, we found this deleterious activity to be almost completely suppressed by inclusion of amino acids or dipeptides, which may suggest a productive relationship between protein and RNA from the outset.

Superactivity of MOF-808 toward Peptide Bond Hydrolysis

MOF-808, a Zr(IV)-based metal-organic framework, has been proven to be a very effective heterogeneous catalyst for the hydrolysis of the peptide bond in a wide range of peptides and in hen egg white lysozyme protein. The kinetic experiments with a series of Gly-X dipeptides with varying nature of amino acid side chain have shown that MOF-808 exhibits selectivity depending on the size and chemical nature of the X side chain. Dipeptides with smaller or hydrophilic residues were hydrolyzed faster than those with bulky and hydrophobic residues that lack electron rich functionalities which could engage in favorable intermolecular interactions with the btc linkers. Detailed kinetic studies performed by 1H NMR spectroscopy revealed that the rate of glycylglycine (Gly-Gly) hydrolysis at pD 7.4 and 60 °C was 2.69 × 10-4 s-1 (t1/2 = 0.72 h), which is more than 4 orders of magnitude faster compared to the uncatalyzed reaction. Importantly, MOF-808 can be recycled several times without significantly compromising the catalytic activity. A detailed quantum-chemical study combined with experimental data allowed to unravel the role of the {Zr6O8} core of MOF-808 in accelerating Gly-Gly hydrolysis. A mechanism for the hydrolysis of Gly-Gly by MOF-808 is proposed in which Gly-Gly binds to two Zr(IV) centers of the {Zr6O8} core via the oxygen atom of the amide group and the N-terminus. The activity of MOF-808 was also demonstrated toward the hydrolysis of hen egg white lysozyme, a protein consisting of 129 amino acids. Selective fragmentation of the protein was observed with 55% yield after 25 h under physiological pH.

HEMIAMINAL-TAG FOR PROTEIN LABELING AND PURIFICATION

The invention pertains to the synthesis, isolation, and characterization of hemiaminal for selective labeling of peptides, proteins, antibodies, and organic fragments with -C(=0) CH2NH2 and derivatives with -CH2NH2 group over -C(=0) CHRNH2 group (where R≠H). The invention also pertains to the method of single-site immobilization of proteins through N-terminus Gly on solid phase. The invention includes late-stage tagging of N-terminus Gly with an affinity tag, 19F NMR probe, and a fluorophore and a method for metal-free protein purification and isolation of analytically pure proteins.

Methanol or formaldehyde ammoxidizing method of synthesizing amide

The invention relates to a methanol or formaldehyde ammoxidizing the method of synthesizing amide. Using methanol or formaldehyde, ammonia and air as the raw materials, in 1-3 gas reactor is continuously carried out in a catalytic reaction, synthesis (C-C) is provided with a carbon-carbon single bond or carbon-carbon-carbon single bond amide (C-C-C) organic compound (called C 2 or C 3 amide, mainly hydroxy acetamide, amino acetamide, diglycolamidic amide, malonamide and nitrilo- three b amide).

Chemical evolution of aminoacetonitrile to glycine under discharge onto primitive hydrosphere: Simulation experiments using glow discharge

Aminoacetonitrile is an important precursor of abiotic amino acids, as shown in the mechanism that was developed to explain the results of the Miller-type spark-discharge experiment. In present experimental setup, a spark discharge is generated in a simulated reducing atmosphere to yield hydrogen cyanide, aldehyde and ammonia; in a second step, a solution-phase reaction proceeds via aminoacetonitrile to give amino acids. However, when the same experiment is carried out in a non-reducing atmosphere, the yield of amino acids is very low. Contact glow discharge electrolysis onto the aqueous phase, which simulates an energy source for chemical evolution, converted aminoacetonitrile via glycinamide to glycine. The mechanism of glycinamide formation was explained by considering the addition of hydrogen and hydroxyl radicals to the C-N triple bond and subsequent transformation into the amide, which was then oxidized to the amino acid. This research suggests that amino acid amides and amino acids can be obtained through oxidation-reduction with H and OH radicals in the primitive hydrosphere whether under reducing or non-reducing conditions.

Development and evaluation of novel phosphotyrosine mimetic inhibitors targeting the Src homology 2 domain of signaling lymphocytic activation molecule (SLAM) associated protein

Specific interactions between Src homology 2 (SH2) domain-containing proteins and the phosphotyrosine-containing counterparts play significant role in cellular protein tyrosine kinase (PTK) signaling pathways. The SH2 domain inhibitors could potentially serve as drug candidates in treating human diseases. Here we have incorporated a novel phosphotyrosine mimetic, which is an unusual amino acid carrying a cyclosaligenyl (cycloSal) phosphodiester moiety, into dipeptides to investigate the inhibitory effect on SH2 domain-containing proteins. A plate-based assay was also established to screen for inhibitors that disrupt the interaction between a phosphopeptide of SLAM (signaling lymphocytic activation molecule) and its interacting protein SAP (SLAM-associated protein). We identified a number of inhibitors with IC50 values in the range of 17-35 μM, implying that the cycloSal phosphodiester-carrying amino acid could mimic the phosphotyrosyl residue. Our results also raise the possibility of integrating the newly developed phosphotyrosine mimetic moiety into inhibitors designed for other SH2 domain-containing proteins.