5241-59-8

Usage

Chemical Properties

Yellowish Solid

Upstream product

• 13033-84-6 D-phenylalanine methyl ester hydrochloride 
• 55379-75-4 2-amino-3-phenylpropanenitrile 
• 15028-44-1 DL-phenylalanine methyl ester 
• 17193-31-6 (R,S)-2-amino-3-phenylpropionamide 
• 71666-94-9 (R)-2-amino-3-phenylpropanamide hydrochloride 
• 513-49-5 (S)-2-aminobutane 
• 13250-12-9 (R)-sec-butylamine 
• 18942-49-9 Boc-D-Phe-OH 
• 129095-62-1 (R)-tert-butyl (1-amino-1-oxo-3-phenylpropan-2-yl)carbamate 
• 108321-83-1 phenylalanine amide hydrochloride 
• 5241-58-7 L-Phenylalanine amide 
• 2448-45-5 Cbz-D-Phe 
• 673-06-3 D-(R)-phenylalanine 
• 155385-80-1 (-)-1-(2-phenyl-ethylideneamino)-2R-methyl-5R-(1-methylethenyl)cyclohexane-1R,3R-dicarbonitrile 

Downstream Products

• 87128-28-7 methyl ester of malonyl-D-phenylalanine amide 
• 74822-65-4 (R)-(+)-1,2-diamino-3-phenylpropane dihydrochloride 
• 1161-13-3 N-Cbz-L-Phe 
• 2448-45-5 Cbz-D-Phe 
• 872035-23-9 (3S,6S,9R,1'R)-3-[9'-fluorenylmethyloxycarbonyl]-9-[(1'-carbamoyl-2'-phenyl)ethyl]carbamoyl-2-oxo-7-thio-1-azabicyclo[4.3.0]nonane 
• 872035-08-0 (2R,5R,11bS,1'R)-2-(tert-butoxycarbonyl)amino-5-[(1'-carbamoyl-2'-phenyl)ethyl]carbamoyl-3-oxo-2,3,5,6,11,11b-hexahydro-1H-indolizino[8,7-b]indole 
• 918881-79-5 (R)-3-phenyl-2-(1-piperidinyl)ethanamide 
• 500767-23-7 (2R,5S,6S)-3-aza-2-benzyl-3-(benzyloxycarbonyl)-6-[(tert-butyloxycarbonyl)amino]-5-hydroxy-7-phenylheptanoyl amide 
• 500767-30-6 (2R,5S,6S)-3-aza-2-benzyl-3-(benzyloxycarbonyl)-6-[[(tert-butyloxycarbonyl)-L-valinyl]amino]-5-hydroxy-7-phenylheptanoyl amide 
• 125482-45-3 (R)-2-[3-(4-Methoxy-phenyl)-oxaziridin-2-yl]-3-phenyl-propionamide 
• 129155-68-6 (R)-2-Hydroxyamino-3-phenyl-propionamide 
• 497865-81-3 (R)-2-bromo-3-phenylpropionic acid D-phenylalaninamide salt 

Relevant academic research and scientific papers

Hybrid catalysis of 8-quinolinecarboxaldehyde and br?nsted acid for efficient racemization of α-amino amides and its application in chemoenzymatic dynamic kinetic resolution

The combination of 8-quinolinecarboxaldehyde and benzoic acid proved to be an effective catalyst system for the racemization of N-unprotected α-aryl- or α-alkyl-substituted α-amino amides. Application of this system to chemoenzymatic dynamic kinetic resolution provided an efficient access to enantiomerically pure N-acetyl-α-amino amides in good to high yields.

Mapping the s1 and s1’ subsites of cysteine proteases with new dipeptidyl nitrile inhibitors as trypanocidal agents

The cysteine protease cruzipain is considered to be a validated target for therapeutic intervention in the treatment of Chagas disease. A series of 26 new compounds were designed, synthesized, and tested against the recombinant cruzain (Cz) to map its S1/S1′ subsites. The same series was evaluated on a panel of four human cysteine proteases (CatB, CatK, CatL, CatS) and Leishmania mexicana CPB, which is a potential target for the treatment of cutaneous leishmaniasis. The synthesized compounds are dipeptidyl nitriles designed based on the most promising combinations of different moieties in P1 (ten), P2 (six), and P3 (four different building blocks). Eight compounds exhibited a Ki smaller than 20.0 nM for Cz, whereas three compounds met these criteria for LmCPB. Three inhibitors had an EC50 value of ca. 4.0 μM, thus being equipotent to benznidazole according to the antitrypanosomal effects. Our mapping approach and the respective structure-activity relationships provide insights into the specific ligand-target interactions for therapeutically relevant cysteine proteases.

Synthetic method for chiral alpha-aminoamide compounds

The invention provides a synthetic method for chiral alpha-aminoamide compounds, belongs to the technical field of organic synthetic methodology, and concretely relates to a synthetic method for chiral alpha-aminoamide compounds, wherein the method has a simple process, low costs and good economy. The method comprises the following steps: 1, performing ammonolysis: adding substituted chiral alpha-aminocarboxylate hydrochloride into concentrated ammonia water, performing stirring for 4-12h under a room temperature, wherein each 1mmol substituted chiral alpha-aminocarboxylate hydrochloride is corresponding to 2-8mL the concentrated ammonia water; 2, after a reaction is finished, performing distillation for removing ammonia water after the reaction to obtain crude products chiral alpha-aminoamide compounds; and 3, performing filtration on the obtained crude products chiral alpha-aminoamide compounds by adopting a manner of adding a solvent or performing purification on the obtained crude products chiral alpha-aminoamide compounds through a manner of column chromatography which uses ammonia water as a mobile phase to obtain the products chiral alpha-aminoamide compounds. Compared with the prior art, a large number of an ammonia gas for ammonolysis is not needed in the method, the process and post-treatment are simple, costs are low and reaction time is short.

Characterization of an enantioselective amidase from Cupriavidus sp. KNK-J915 (FERM BP-10739) useful for enzymatic resolution of racemic 3-piperidinecarboxamide

A novel amidase (CsAM) acting on (R,S)-N-benzyl-3-piperidinecarboxamide was purified from Cupriavidus sp. KNK-J915 (FERM BP-10739) and characterized. The enzyme acts on (R,S)-N-benzyl-3-piperidinecarboxamide S-selectively to yield (R)-N-benzyl-3-piperidinecarboxamide. Analytical gel filtration column chromatography and SDS-PAGE revealed that the enzyme is a tetramer with a subunit of approximately 47 kDa. It has a broad substrate spectrum against nitrogen-containing heterocyclic amides. Its optimal pH and temperature are 8.0-9.0 and 50 °C, respectively. The CsAM gene was cloned and sequenced, and it was found to comprise 1341 bp and encode a polypeptide of 46,388 Da. The deduced amino acid sequence exhibited 78% identity to that of a putative amidase (CnAM) from Cupriavidus necator JMP134. The cultured cells of recombinant Escherichia coli producing CnAM could be used for the S-selective hydrolysis of (R,S)-N-benzyl-3-piperidinecarboxamide but could not be used for the S-selective hydrolysis of (R,S)-3-piperidinecarboxamide because of its very low level of selectivity. In contrast, the cultured cells of recombinant E. coli producing CsAM could hydrolyze both (R,S)-N-benzyl-3-piperidinecarboxamide and (R,S)-3-piperidinecarboxamide with high S-selectivity.

2-(N-Benzyl-N-phenylsulfonamido)alkyl amide derivatives as γ-secretase inhibitors

A series of (N-benzyl-N-phenylsulfonamido)alkyl amides were developed from classic and parallel synthesis strategies. Compounds with good in vitro and in vivo γ-secretase activity were identified and described.

Carbamates of 4′-demethyl-4-deoxypodophyllotoxin: Synthesis, cytotoxicity and cell cycle effects

In an attempt to generate compounds with superior bioactivity and reduced toxicity, 12 carbamates of 4′-demethyl-4-deoxypodophyllotoxin, N-(1-oxyl-4′-demethyl- 4-deoxypodophyllic)-α-amino acids amides, were synthesized and evaluated for antiproliferative activity and cell cycle effects. These synthesized compounds proved to be more hydrophilic, as well as improved or comparable in vitro cytotoxicities against four cell lines (A-549, HeLa, SiHa, and HL-60) compared with either parent DPT or anti-cancer drug VP-16. Furthermore, flow cytometric analysis exhibited that N-(1-oxyl-4′- demethyl-4-deoxypodophyllic)-d-α-methine amide (15f) induced cell cycle arrest in the G2/M phase in A-549 cells.

Structure-based design of novel human Pin1 inhibitors (II)

Following the discovery of a novel series of phosphate-containing small molecular Pin1 inhibitors, the drug design strategy shifted to replacement of the phosphate group with an isostere with potential better pharmaceutical properties. The initial loss in potency of carboxylate analogs was likely due to weaker charge-charge interactions in the putative phosphate binding pocket and was subsequently recovered by structure-based optimization of ligand-protein interactions in the proline binding site, leading to the discovery of a sub-micromolar non-phosphate small molecular Pin1 inhibitor.

Enantiopure trans -3-arylaziridine-2-carboxamides: Preparation by bacterial hydrolysis and ring-openings toward enantiopure, unnatural D -α-amino acids

Several racemic trans-3-arylaziridine-2-carboxamides were prepared and then resolved by Rhodococcus rhodochrous IFO 15564-catalyzed hydrolysis. The resulting enantiopure (2R,3S)-3-arylaziridine-2-carboxamides are adequate substrates to undergo fully stereoselective nucleophilic ring-openings at the C-3 ring position to finally yield enantiopure, unnatural d-α- aminocarboxylic acids. Experimental evidence is provided that suggests the fate of the (2S,3R)-3-arylaziridine-2-carboxylic acids concomitantly formed during the resolution processes. In this context, the similar bacterial resolution of racemic 1-arylaziridine-2-carboxamides and -carbonitriles, previously investigated by our research group, has been partially re-examined.

Induced-fit in the gas phase: Conformational effects on the enantioselectivity of chiral tetra-amide macrocycles

The structure, stability, and reactivity of proton-bound diastereomeric [M?H?A]+ complexes between some amino acid derivatives (A) and several chiral tetra-amide macrocycles (M) have been investigated in the gas phase by ESI-FT-ICR and ESI-ITMS-CID mass spectrometry. The displacement of the A guest from the diastereomeric [M?H?A]+ complexes by reaction with the 2-aminobutane enantiomers (B) exhibits a distinct enantioselectivity with regards to the leaving amino acid A and, to a minor extent, to the amine reactant B. The emerging selectivity picture, discussed in the light of molecular mechanics calculations, provides compelling evidence that the most stable conformers of the selected chiral tetraamide macrocycles M may acquire in the gas phase a different conformation by induced fit on complexation with some representative amino acid derivatives A. This leads to the coexistence in the gas phase of stable diastereomeric [M?H?A] + eq-eq and ax-ax structures, in proportions depending on the configuration of A and M and characterized by different stability and reactivity toward the 2-aminobutane enantiomers. The enantioselectivity of the gas-phase A-to-B displacement in the diastereomeric [M?H?A]+ complexes essentially reflects the free energy gap between the homo- and heterochiral [M?H?A]+ complexes, except when the tetra-amidic host presents an additional macrocycle generated by a decamethylene chain. In this case, the measured enantioselectivity mostly reflects the stability difference between the relevant diastereomeric transition structures.

Nitrile and amide biotransformations for the synthesis of enantiomerically pure 3-arylaziridine-2-carboxamide derivatives and their stereospecific ring-opening reactions

(Chemical Equation Presented) Catalyzed by Rhodococcus erythropolis AJ270 (whole cell catalyst) under very mild conditions, a number of racemic trans-3-arylaziridine-2-carbonitriles and amides were efficiently transformed into enantiopure 2R,3S-3-arylazir