72155-45-4

Usage

Uses

Used in Pharmaceutical Industry:
N-Boc-L-phenylalaninal is used as a potent human cathepsin K inhibitor for the development of therapeutic agents targeting bone resorption and osteoporosis. It plays a crucial role in modulating the activity of cathepsin K, a protease enzyme involved in bone remodeling and degradation.
Used in Chemical Synthesis:
N-Boc-L-phenylalaninal is used as an intermediate for the synthesis of hydroxyethylene dipeptide isosteres, which possess enzyme inhibition properties. These isosteres are valuable in the development of novel drugs and bioactive compounds with improved pharmacological profiles.
Used in Research and Development:
As a synthetic amino aldehyde, N-Boc-L-phenylalaninal is employed in research and development for the design and synthesis of various bioactive molecules, including peptides, peptidomimetics, and other small molecule inhibitors. Its unique chemical properties make it a valuable building block in medicinal chemistry and drug discovery.

InChI:InChI=1/C14H19NO3/c1-14(2,3)18-13(17)15-12(10-16)9-11-7-5-4-6-8-11/h4-8,10,12H,9H2,1-3H3,(H,15,17)/t12-/m1/s1

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 51987-73-6 (S)-2-tert-butoxycarbonylamino-3-phenyl-propionic acid methyl ester 
• 66605-57-0 (S)-N-tert-butoxycarbonyl-2-amino-3-phenylpropanol 
• 142955-51-9 N-butoxycarbonyl-L-phenylalanine anhydride 
• 120125-44-2 N^α-(tert-butoxycarbonyl)-L-phenylalanine-N-morpholinamide 
• 24424-99-5 di-tert-butyl dicarbonate 
• 4522-04-7 ethyl N-{[(1,1-dimethylethyl)oxy]carbonyl}-L-phenylalaninate 
• 63-91-2 L-phenylalanine 
• 3182-95-4 L-Phenylalaninol 
• 67729-36-6 Boc-Phe-O-COO-isoBu 
• 38862-25-8 methacrylic acid N-hydroxysuccinimide ester 
• 1073536-45-4 (S)-tert-butyl 1,1-bis(ethylthio)-3-phenylpropan-2-ylcarbamate 
• 34101-07-0 (2S)-2-[N-(tert-butoxycarbonyl)amino]-1-imidazol-1-yl-3-phenylpropan-1-one 
• 133489-47-1 (S)-2-amino-N-methoxy-N-methyl-3-phenylpropanamide 

Downstream Products

• 143327-79-1 ((S)-1-benzyl-2-prop-2-ynyl)carbamic acid t-butyl ester 
• 130832-45-0 [(1S,2S)-1-Benzyl-2-hydroxy-2-(6-hydroxy-benzo[1,3]dioxol-5-yl)-ethyl]-carbamic acid tert-butyl ester 
• 130832-46-1 [(1S,2R)-1-Benzyl-2-hydroxy-2-(6-hydroxy-benzo[1,3]dioxol-5-yl)-ethyl]-carbamic acid tert-butyl ester 
• 145473-32-1 [1-Benzyl-2-hydroxy-2-(2-oxo-cyclooctyl)-ethyl]-carbamic acid tert-butyl ester 
• 98760-08-8 (2R,3S)-3-[N-(tert-butyloxycarbonyl)amino]-1,2-epoxy-4-phenylbutane 
• 98760-08-8 (1-oxiranyl-2-phenylethyl)carbamic acid tert-butyl ester 
• 161282-72-0 (2S,3R)-N-tert-butyloxycarbonyl-2-amino-3-hydroxy-1-phenyl-4-nitrobutane 
• 174302-74-0 (2S,3S)-N-tert-butyloxycarbonyl-2-amino-3-hydroxy-1-phenyl-4-nitrobutane 
• 159141-35-2 [(1S,2R)-1-Benzyl-2-((S)-1-carbamoyl-3-methyl-butylamino)-2-cyano-ethyl]-carbamic acid tert-butyl ester 
• 159247-02-6 [(1S,2S)-1-Benzyl-2-((S)-1-carbamoyl-3-methyl-butylamino)-2-cyano-ethyl]-carbamic acid tert-butyl ester 

Relevant academic research and scientific papers

Amino acid based synthesis of chiral long chain diamines and tetramines

A method for the synthesis of long chain diamines and tetramines starting from natural α-amino acids is reported. Diamines and tetramines were prepared through the Wittig olefination reaction of N-protected amino aldehydes obtained from phenylalanine and lysine. A 1,2,17,18-tetramine was synthesized using (2S)-1-azido-2-[bis(tert-butoxycarbonyl)-amino]-5-oxopentane as key-intermediate compound.

PADAM reactions of α-aminoaldehydes: Identity of major and minor diastereomers from the Passerini reaction

The Passerini reaction was conducted using N-Boc-L-phenylalaninal and a variety of achiral or chiral acids and isocyanides to prepare a library of 27 Passerini products. Reaction diastereoselectivity varied between 1.7:1 and 2.5:1 and in most cases isolat

Design, Synthesis, and Cytotoxic Activity of New Tubulysin Analogues

Synthesis of tubulysin analogues, containing an N-methyl substituent on tubuvaline-amide together with the replacement of either the hydrophobic N-terminal N-methyl pipecolic acid (Mep) or at both N- and C- terminal peptides with available heteroaromatic

Probing α-Amino Aldehydes as Weakly Acidic Pronucleophiles: Direct Access to Quaternary α-Amino Aldehydes by an Enantioselective Michael Addition Catalyzed by Br?nsted Bases

The high tendency of α-amino aldehydes to undergo 1,2-additions and their relatively low stability under basic conditions have largely prevented their use as pronucleophiles in the realm of asymmetric catalysis, particularly for the production of quaternary α-amino aldehydes. Herein, it is demonstrated that the chemistry of α-amino aldehydes may be expanded beyond these limits by documenting the first direct α-alkylation of α-branched α-amino aldehydes with nitroolefins. The reaction produces densely functionalized products bearing up to two, quaternary and tertiary, vicinal stereocenters with high diastereo- and enantioselectivity. DFT modeling leads to the proposal that intramolecular hydrogen bonding between the NH group and the carbonyl oxygen atom in the starting α-amino aldehyde is key for reaction stereocontrol.

Potent Anti-SARS-CoV-2 Activity by the Natural Product Gallinamide A and Analogues via Inhibition of Cathepsin L

Cathepsin L is a key host cysteine protease utilized by coronaviruses for cell entry and is a promising drug target for novel antivirals against SARS-CoV-2. The marine natural product gallinamide A and several synthetic analogues were identified as potent inhibitors of cathepsin L with IC50 values in the picomolar range. Lead molecules possessed selectivity over other cathepsins and alternative host proteases involved in viral entry. Gallinamide A directly interacted with cathepsin L in cells and, together with two lead analogues, potently inhibited SARS-CoV-2 infection in vitro, with EC50 values in the nanomolar range. Reduced antiviral activity was observed in cells overexpressing transmembrane protease, serine 2 (TMPRSS2); however, a synergistic improvement in antiviral activity was achieved when combined with a TMPRSS2 inhibitor. These data highlight the potential of cathepsin L as a COVID-19 drug target as well as the likely need to inhibit multiple routes of viral entry to achieve efficacy.

Application of proteasome inhibitor in inhibition of novel coronavirus

The invention provides application of a proteasome inhibitor in inhibition of a novel coronavirus or preparation of novel coronavirus inhibitors. The proteasome inhibitor has a structure represented by a formula (I) or isomers, pharmaceutically acceptable salts thereof and prodrugs thereof. According to the application, by applying the proteasome inhibitor to inhibition of the novel coronavirus, good inhibiting activity is obtained, and a novel treatment way of think is provided for diseases such as pneumonia caused by the novel coronavirus.

Vinyl sulfone-based inhibitors of trypanosomal cysteine protease rhodesain with improved antitrypanosomal activities

The number of reported cases of Human African Trypanosmiasis (HAT), caused by kinetoplastid protozoan parasite Trypanosoma brucei, is declining in sub-Saharan Africa. Historically, such declines are generally followed by periods of higher incidence, and one of the lingering public health challenges of HAT is that its drug development pipeline is historically sparse. As a continuation of our work on new antitrypanosomal agents, we found that partially saturated quinoline-based vinyl sulfone compounds selectively inhibit the growth of T. brucei but displayed relatively weak inhibitory activity towards T. brucei's cysteine protease rhodesain. While two nitroaromatic analogues of the quinoline-based vinyl sulfone compounds displayed potent inhibition of T. brucei and rhodesain. The quinoline derivatives and the nitroaromatic-based compounds discovered in this work can serve as leads for ADME-based optimization and pre-clinical investigations.

Total synthesis of tubulysin U and N14-desacetoxytubulysin H

A concise and efficient procedure for the total synthesis of tubulysin U and N14-desacetoxytubulysin H has been developed with high stereoselectivity on a gram scale. This synthesis features an elegant cascade one-pot process to install the challenging th

Vinyl Sulfone-Based Inhibitors of Nonstructural Protein 2 Block the Replication of Venezuelan Equine Encephalitis Virus

Emerging infectious diseases like those caused by arboviruses such as Venezuelan equine encephalitis virus (VEEV) pose a serious threat to public health systems. Development of medical countermeasures against emerging infectious diseases are of utmost importance. In this work, an acrylate and vinyl sulfone-based chemical series was investigated as promising starting scaffolds against VEEV and as inhibitors of the cysteine protease domain of VEEV's nonstructural protein 2 (nsP2). Primary screen and dose response studies were performed to evaluate the potency and cytotoxicity of the compounds. The results provide structural insights into a new class of potent nonpeptidic covalent inhibitors of nsP2 cysteine protease represented by compound 11 (VEEV TrD, EC50= 2.4 μM (HeLa), 1.6 μM (Vero E6)). These results may facilitate the evolution of the compounds into selective and broad-spectrum anti-alphaviral drug leads.

Peptidomimetic Vinyl Heterocyclic Inhibitors of Cruzain Effect Antitrypanosomal Activity

Cruzain, an essential cysteine protease of the parasitic protozoan, Trypanosoma cruzi, is an important drug target for Chagas disease. We describe here a new series of reversible but time-dependent inhibitors of cruzain, composed of a dipeptide scaffold appended to vinyl heterocycles meant to provide replacements for the irreversible reactive "warheads" of vinyl sulfone inactivators of cruzain. Peptidomimetic vinyl heterocyclic inhibitors (PVHIs) containing Cbz-Phe-Phe/homoPhe scaffolds with vinyl-2-pyrimidine, vinyl-2-pyridine, and vinyl-2-(N-methyl)-pyridine groups conferred reversible, time-dependent inhibition of cruzain (Ki? = 0.1-0.4 μM). These cruzain inhibitors exhibited moderate to excellent selectivity versus human cathepsins B, L, and S and showed no apparent toxicity to human cells but were effective in cell cultures of Trypanosoma brucei brucei (EC50 = 1-15 μM) and eliminated T. cruzi in infected murine cardiomyoblasts (EC50 = 5-8 μM). PVHIs represent a new class of cruzain inhibitors that could progress to viable candidate compounds to treat Chagas disease and human sleeping sickness.