14235-15-5

Basic information

• Product Name: Carbamic acid, [(1R)-2-[(4-nitrophenyl)amino]-2-oxo-1-(phenylmethyl)ethyl]-, phenylmethyl ester
• CAS NO: 14235-15-5
• Molecular Formula: C23H21N3O5
• Molecular Weight: 419.437
• Mol File: 14235-15-5.mol
• Article Data: 10

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [(1R)-2-[(4-nitrophenyl)amino]-2-oxo-1-(phenylmethyl)ethyl]-, phenylmethyl ester(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [(1R)-2-[(4-nitrophenyl)amino]-2-oxo-1-(phenylmethyl)ethyl]-, phenylmethyl ester(14235-15-5)
• EPA Substance Registry System: Carbamic acid, [(1R)-2-[(4-nitrophenyl)amino]-2-oxo-1-(phenylmethyl)ethyl]-, phenylmethyl ester(14235-15-5)

Safety Data

• Hazardous Substances Data: 14235-15-5(Hazardous Substances Data)

Upstream product

• 2448-45-5 Cbz-D-Phe 
• 100-01-6 4-nitro-aniline 
• 1161-13-3 N-Cbz-L-Phe 
• 134393-23-0 N,N'-bis(4-nitrophenyl)phospheneimidous amide 

Downstream Products

• 14235-18-8 H-D-Phe-pNA 
• 1161-13-3 N-Cbz-L-Phe 
• 1361510-35-1 (S)-benzyl 1-(4-nitrophenylamino)-3-phenyl-1-selenoxopropan-2-ylcarbamate 
• 100-01-6 4-nitro-aniline 
• 776253-75-9 H-L-Tyr-D-Leu-D-Phe-pNA 
• 99242-14-5 Boc-D-Leu-D-Phe-pNA 
• 99242-15-6 H-D-Leu-D-Phe-pNA 
• 99242-09-8 Suc-L-Tyr-D-Leu-D-Phe-pNA 
• 99242-16-7 Boc-L-Tyr-D-Leu-D-Phe-pNA 
• 102292-75-1 Boc-D-Leu-L-Phe-pNA 
• 99242-15-6 H-D-Leu-L-Phe-pNA 
• 99251-92-0 Suc-L-Tyr-D-Leu-L-Phe-pNA 
• 102292-77-3 Boc-L-Tyr-D-Leu-L-Phe-pNA 
• 75651-89-7 H-Leu-Phe-pNA*HCl 

Relevant articles and documents

Amidase activity of phosphonate analogue imprinted chymotrypsin mimics in shape-selective, substrate-specific and enantioselective amidolysis of l-phenylalanine-p-nitroanilides

Focusing on chymotrypsin mimics, highly crosslinked enzyme mimics are synthesized by molecular imprinting technique for the amidolysis of p-nitroanilide of phenylalanine, using phenyl-1-(N-benzyloxycarbonylamino)-2-(phenyl)ethyl phosphonate - the transition state analog of amidolysis - as the template, N-methacryloyl-l-histidine, N-methacryloyl-l-aspartic acid, and N-methacryloyl-l-serine as the functional monomers and EGDMA as the crosslinking agent. The amidase activity of the enzyme mimics follows pseudo first order kinetics. The transition state analog provides a tetrahedral geometry complementary to the transition state intermediate, which is responsible for the catalytic activity of the imprinted enzyme mimics. The enzyme mimics show stereospecificity and substrate selectivity in the amidolysis of phenylalanine p-nitroanilide. The proper orientation of the reactive functionalities in the super crosslinked macroporous polymer matrix for selective binding of the substrate through H-bonding is responsible for the high imprinting efficiency and substrate specificity of the imprinted polymer catalysts. Low cost, ease of preparation, high thermal stability, reusability and higher shelf life make the polymer catalysts better chymotrypsin mimics.

Synthesis of selenoxo peptides and oligoselenoxo peptides employing LiAlHSeH

Synthesis of selenoxo peptides by the treatment of Nα- protected peptide esters with a combination of PCl5 and LiAlHSeH is delineated. The method is simple, high-yielding, and free from racemization. Thus obtained selenoxo peptides are used as units for N-terminal chain extension through Nα-deprotection/coupling to yield peptide-selenoxo peptide hybrids. Multiple selenation is demonstrated by conversion of two peptide bonds of tripeptides into selenoxo peptide bonds. Amino acid derived arylamides are also converted into aryl selenoamides. C6H 5-CSeNH-Val-OMe 8f is obtained as single crystal, and its structure was determined through X-ray diffraction study.