4854-49-3

Usage

General Description

2-acetamido-2-phenylpropanoic acid is a chemical compound with the molecular formula C11H13NO3. It is a derivative of phenylpropanoic acid, which is commonly used as a non-steroidal anti-inflammatory drug (NSAID) for pain relief and reducing inflammation. 2-acetamido-2-phenylpropanoic acid contains an acetamide group and a phenyl group attached to the central carbon atom, making it a chiral molecule with potential pharmaceutical and biological applications. The presence of the acetamide group allows it to interact with enzymes and receptors in the body, potentially affecting various physiological processes. Its chemical structure and interactions make it a promising candidate for further research and development in the field of pharmaceuticals.

Upstream product

• 124-38-9 carbon dioxide 
• 57957-24-1 N-(1-phenylvinyl)acetamide 
• 171181-53-6 methyl N^α-(diphenylmethylene)-DL-phenylglycinate 
• 565-07-1 2-amino-2-phenylpropanoic acid 
• 108-24-7 acetic anhydride 

Downstream Products

• 4855-22-5 2,4-dimethyl-4-phenyl-Δ²-oxazolin-5-one 
• 156175-19-8 2-acetylamino-2-phenyl-2'-phenylpropionohydrazide 

Relevant academic research and scientific papers

Selective and Catalytic Hydrocarboxylation of Enamides and Imines with CO2 to Generate α,α-Disubstituted α-Amino Acids

The first catalytic hydrocarboxylation of enamides and imines with CO2 to generate valuable α,α-disubstituted α-amino acids is reported. Notably, excellent chemo- and regio-selectivity are achieved, significantly different from previous reports

Structure-Activity Study of Tripeptide Thrombin Inhibitors Using α-Alkyl Amino Acids and Other Conformationally Constrained Amino Acid Substitutions

In our continuing effort to design novel thrombin inhibitors, a series of conformationally constrained amino acids (e.g. α-alkyl, N-alkyl cyclic, etc.) were utilized in a systematic structure-activity study of the P3, P2, and P1 positions of tripeptide arginal thrombin inhibitors.Early examples of this effort include: D-MePhe-Pro-Arg-H (15), Boc-D-Phg-Pro-Arg-H (18), D-1-Tiq-Pro-Arg-H (23, D-1-Tiq = D-1,2,3,4-tetrahydroisoquinolin-1-ylcarbonyl), and Boc-D-Phe-Pro-Arg-H (25).10a,20 The current work clarifies the contribution of each residue of the tripeptide arginals toward the potent and selective inhibition of thrombin relative to that of t-PA and plasmin.The α-methylarginal modification in the P1 residue resulted in analogs 30 (D-MePhe at P3) and 32 (D-1-Tiq at P3) which had lower potency toward thrombin while exhibiting improved selectivity.Analogs modified at the P2 site were found to be very sensitive to the conformational changes induced by variations in side chain ring size with the flexible pipecolinic acid 31 being 2 orders of magnitude less potent at thrombin inhibition than the conformationally constrained azetidine analog 20.Examination of the P3 binding region indicated that α-alkylphenylglycine residues resulted in a tendency to exhibit substantional improvements in selectivity over the nonalkylated residues.Combinations of optimal P3 and P2 changes led to compounds TFA-D-Phg(αEt)-Azt-Arg-H (16), TFA-D-Phg(αMe)-Azt-Arg-H (17), Ac-D-Phg(αMe)-Azt-Arg-H (21), TFA-D-Phg(αMe)-Pro-Arg-H (27), 30, and 32, which are clearly more selective for thrombin versus plasmin than the nonconformationally constrained compounds.