14440-98-3

Usage

Uses

Used in Pharmaceutical Industry:
N-[(Benzyloxy)carbonyl]-3-phenyl-beta-alanine is used as a synthetic intermediate for the development of protease inhibitors. These inhibitors play a crucial role in the treatment of various diseases, including cancer and viral infections, by blocking the action of proteases, which are essential for the replication and survival of these diseases.
Additionally, N-[(Benzyloxy)carbonyl]-3-phenyl-beta-alanine is used in the synthesis of DL-β-Phenylalanine N-Hydroxysuccinimide Ester (P319400), which is another important compound in the pharmaceutical industry. This ester has potential applications in the development of new drugs and therapeutic agents, further highlighting the versatility of Cbz-DL-β-phenylalanine in the pharmaceutical field.

Upstream product

• 122-97-4 3-Phenyl-1-propanol 
• 140-10-3 (E)-3-phenylacrylic acid 
• 355145-63-0 (+/-)-4-phenyl-tetrahydro-1,2,3-oxathiazine-2,2-dioxide 
• 136199-49-0 3-phenylpropyl sulfamate 
• 5491-18-9 (S)-N-(benzyloxycarbonyl)phenylglycine 
• 228861-79-8 N^α-Z-phenylglycinyldiazomethane 
• 355145-65-2 2,2-dioxo-4-phenyl-2λ⁶-[1,2,3]oxathiazinane-3-carboxylic acid benzyl ester 
• 3646-50-2 3-Amino-3-phenylpropionic acid 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 149193-92-0 3-Amino-3-phenyl-propionic acid tert-butyl ester 
• 1609650-84-1 Cbz-D,L-β-Phe-Bt 
• 1609650-87-4 Cbz-D,L-β-Phe-D-Pro-OH 
• 1609651-13-9 cyclo-(β-Ala-D-Pro-D,L-β-Phe-D-Pro) 
• 1609656-90-7 cyclo-(D,L-β-Phe-D-Pro-)₂ 
• 1043434-45-2 C₂₁H₂₄N₂O₃ 
• 1098022-30-0 3'-(N-benzyloxycarbonyl-β-phenyl-β-dl-alanyl)amino-3'-deoxy-thymidine 
• 46050-30-0 3-amino-3-phenylpropanamide 
• 138261-26-4 (1'S,6S)-1-(benzyloxycarbonyl)-3-(1'-phenyleth-1'-yl)-6-phenylperihydropyrimidin-4-one 
• 138261-27-5 (1'S,6R)-1-(benzyloxycarbonyl)-3-(1'-phenyleth-1'-yl)-6-phenylperihydropyrimidin-4-one 
• 854885-59-9 3-benzyloxycarbonylamino-3-phenyl-propionyl chloride 
• 17193-27-0 N^β-Benzyloxycarbonyl-DL-β-phenyl-β-alanin-amid 

Relevant academic research and scientific papers

MODULATORS OF CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR

This disclosure provides modulators of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR), pharmaceutical compositions containing at least one such modulator, methods of treatment of cystic fibrosis using such modulators and pharmaceutical compositions, and processes for making such modulators.

A novel, microwave-assisted method for the synthesis of alicyclic-condensed 5H-1,4,6,7-tetrahydro-1,4-diazepin-5-ones

An efficient, high-yielding method has been developed for the synthesis of cycloalkane-fused and phenyl-substituted 1,4-diazepin-5-ones from β-amino acids. The process involves the oxidative cleavage of a terminal olefin bond and an acid-catalyzed, microw

Inhibitors interacting with the magnesium binding site of reverse transcriptase: Synthesis and biological activity studies of 3′-(Ω- amino-acyl) amino-3′-deoxy-thymidine

Active site of reverse transcriptase contains carboxylate groups involved in the magnesium binding. We prepared some nucleoside analogs which could bind to these carboxylates preventing the binding of nucleotides. To the 3′-amino-3′-deoxy-thymidine, different N-protected ω-amino-acids were bound, the protection removed to give the 3′-(ω-amino-acyl-) amino-3′-deoxy-thymidines in good yield. Some showed moderate to low activity in HIV 1 replication test. Copyright Taylor & Francis Group, LLC.

Effective methods for the synthesis of N-methyl β-amino acids from all twenty common α-amino acids using 1,3-oxazolidin-5-ones and 1,3-oxazinan-6-ones

N-Methyl β-amino acids are generally required for application in the synthesis of potentially bioactive modified peptides and other oligomers. Previous work highlighted the reductive cleavage of 1,3-oxazolidin-5-ones to synthesise N-methyl α-amino acids. Starting from α-amino acids, two approaches were used to prepare the corresponding N-methyl β-amino acids. First, α-amino acids were converted to N-methyl α-amino acids by the so-called '1,3-oxazolidin-5-one strategy', and these were then homologated by the Arndt-Eistert procedure to afford N-protected N-methyl β-amino acids derived from the 20 common α-amino acids. These compounds were prepared in yields of 23-57% (relative to N-methyl α-amino acid). In a second approach, twelve N-protected α-amino acids could be directly homologated by the Arndt-Eistert procedure, and the resulting β-amino acids were converted to the 1,3-oxazinan-6-ones in 30-45% yield. Finally, reductive cleavage afforded the desired N-methyl β-amino acids in 41-63% yield. One sterically congested β-amino acid, 3-methyl-3-aminobutanoic acid, did give a high yield (95%) of the 1,3-oxazinan-6-one (65), and subsequent reductive cleavage gave the corresponding AIBN-derived N-methyl β-amino acid 61 in 71% yield (Scheme 2). Thus, our protocols allow the ready preparation of all N-methyl β-amino acids derived from the 20 proteinogenic α-amino acids.

ANTITHROMBOTIC AGENTS

This invention relates to L-Arginine aldehyde derivatives, pharmaceutical formulations containing those compounds and methods of their use as thrombin inhibitors, coagulation inhibitors and thromboembolic disorder agents.

Highly diastereoselective alkylation of perhydropyrimidin-4-ones directed toward the synthesis of α-substituted β-amino acids. 2

The alkylation of several enantiomerically pure perhydropyrimidin-4-ones at C5 is described. For the methylation reaction, mixtures of 5,6-trans -and cis-disubstituted adducts were obtained with high diastereomeric ratios, whereas only the 5,6-

Analogues of 2'(3')-O-L-phenylalanyladenosine as substrates and inhibitors of ribosomal peptidyltransferase

The chemical syntheses of 2'(3')-O-(L-3-amino-3-phenylpropionyl)adenosine (2e), the corresponding D stereoisomer 2f, 2'(3')-O-(DL-phenylglycyl)adenosine (2g), 2'(3')-O-(N-benzylglycyl)adenosine (2h), and 9-(2-O-L-phenylalanyl-β-D-xylofuranosyl)adenine (3b) are described. Compounds 2e-h were obtained by acylation of 5'-O(4-methoxytrityl)adenosine with the appropriate N-benzyloxycarbonyl or N-tert-butoxycarbonyl amino acids with dicyclohexylcarbodiimide in pyridine. The corresponding reaction of N-(benzyloxycarbonyl)-D-phenylglycine led to an almost complete racemization of the aminoacyl residue (compounds 2c and 2g). Subsequent chromatographic separation and deprotection of intermediates 2a-d afforded the desired target derivatives 2e-h. Product 3b was obtained by a similar acylation of 9-(3,5-O-isopropylidene-β-D-xylofuranosyl)adenine with N-(benzyloxycarbonyl)-L-phenylalanine, followed by deblocking. The NMR spectra of 2' and 3' isomers of stereoisomers 2a and 2b are discussed. Compounds 2g and 3b are both substrates and inhibitors of Escherichia coli ribosomal peptidyltransferase, although the activity of 3b is low. Derivatives 2e,f,h do not accept AcPhe from N-AcPhe-tRNA in a peptidyltransferase-catalyzed reaction, but they inhibit the puromycin reaction in the same system. The order of inhibitory activity is 2e>2f>2h. The implications of these findings for the mechanism of peptidyltransferase and comparison of the latter with the action of chymotrypsin are discussed.