15962-47-7

Usage

Chemical Properties

White to off-white powder

Purification Methods

Crystallise the amide repeatedly from EtOH/diethyl ether. The (±)-isomer crystallises from H2O and has m 157-158o. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 p 1838 1961. de Jong Recl Trav Chim Pays-Bas 19 288 1900, Fischer & Otto Chem Ber 36 2106 1903, Beilstein 4 H 295.]

InChI:InChI=1/C5H10N2O2/c1-3(5(6)9)7-4(2)8/h3H,1-2H3,(H2,6,9)(H,7,8)/t3-/m0/s1

Upstream product

• 60-35-5 acetamide 
• 78-97-7 2-hydroxy-propionitrile 
• 617-35-6 2-oxo-propionic acid ethyl ester 
• 1115-69-1 Ac-DL-Ala 
• 5686-40-8 (S)-N-ethanoylalanine ethyl ester 
• 108-24-7 acetic anhydride 
• 13139-27-0 L-α-N-Cbz-alaninamide 
• 97-69-8 (S)-acetamidoalanine 

Downstream Products

• 1051922-96-3 C₁₃H₂₀N₂O₄ 
• 19861-71-3 (S)-N-(1-cyanoethyl)acetamide 
• 1369514-64-6 methyl 2-(2-acetamidopropanamido)-3-methyl-6-phenylfuro[3,2-b]pyrazine-7-carboxylate 
• 1369514-59-9 methyl 2-(2-acetamidopropanamido)-6-phenylfuro[3,2-b]pyrazine-7-carboxylate 

Relevant academic research and scientific papers

PH-Dependent peptide bond formation by the selective coupling of α-amino acids in water

A novel mechanism enabling selective peptide elongation by coupling α-amino acids over other potentially competing prebiotic amines under acidic aqueous condition is suggested. It proceeds via the generation of a carboxylic acid anhydride intermediate with subsequent intramolecular formation of the amide bond. This journal is

Oxidative Damage in Aliphatic Amino Acids and Di- and Tripeptides by the Environmental Free Radical Oxidant NO3?: the Role of the Amide Bond Revealed by Kinetic and Computational Studies

Kinetic and computational data reveal a complex behavior of the important environmental free radical oxidant NO3? in its reactions with aliphatic amino acids and di- and tripeptides, suggesting that attack at the amide N-H bond in the peptide backbone is a highly viable pathway, which proceeds through a proton-coupled electron transfer (PCET) mechanism with a rate coefficient of about 1 × 106 M-1 s-1 in acetonitrile. Similar rate coefficients were determined for hydrogen abstraction from the α-carbon and from tertiary C-H bonds in the side chain. The obtained rate coefficients for the reaction of NO3? with aliphatic di- and tripeptides suggest that attack occurs at all of these sites in each individual amino acid residue, which makes aliphatic peptide sequences highly vulnerable to NO3?-induced oxidative damage. No evidence for amide neighboring group effects, which have previously been found to facilitate radical-induced side-chain damage in phenylalanine, was found for the reaction of NO3? with side chains in aliphatic peptides.

Direct, facile synthesis of N-acyl-α-amino amides from α-keto esters and ammonia

N-Acyl-α-amino amides were prepared, without the necessity of chromatographic purification, in a single step by heating the corresponding α-keto ester in methanolic ammonia. The Royal Society of Chemistry.

Interactions between Terminally Substituted Amino Acids in an Aqueous and a Non-Aqueous Environment. Enthalpic Interaction Coefficients in Water and in N,N-Dimethylformamide at 25 deg C

Enthalpies of dilution of the N-acetyl amides of glycine, L-alanine, L-valine, L-leucine, and L-phenylalanine, dissolved in N,N-dimethylformamide (DMF) as a solvent have been measured at 25 deg C.The results obtained have been analyzed to give the enthalpic interaction (or virial) coefficients of the solutes and these are compared with information previously obtained in aqueous systems.There are marked differences in the interaction properties in the two solvents and, while the additivity approache of Savage and Wood is applicable to the solutes in water it is suitable for representing the interactions in DMF.A correlation is presented between the enthalpic second virial coefficients in DMF and the propensity of side-chains to be in proximity in globular proteins.

Aqueous Solutions Containing Amino Acids and Peptides. Part 11.-Enthalpy of Dilution of Single and Binary Solute Solutions of N-Acetylglycine Amide, N-Acetyl-L-alanine Amide, N-Acetyl-L-valine Amide and N-Acetyl-L-leucine Amide at 298.15 K

The enthalpies of dilution of aqueous solutions containing N-acetylglycine amide (G), N-acetyl-L-alanine amide (A), N-acetyl-L-valine amide (V) and N-acetyl-L-leucine amide (L) and equimolal solutions of G+A, G+V, G+L, A+V, A+L and V+L have been measured at 298.15 K.The results obtained have been used to calculate the pairwise enthalpy coefficients for like-like and like-unlike solute interactions.These coefficients have been compared with the predictions of the group additivity approach proposed earlier by Savage and Wood.The group additivity approach works well considering the experimental error and the standard deviation of the original correlations although it seems likely that some refinement of the group interaction parameters is required.