490034-62-3

Usage

Uses

Used in Biochemical Research:
H-Phe(2-Me)-OH.HCl is used as a research tool for [enhancing the understanding of protein structure and function] because of its ability to modulate the activity of proteins and enzymes.
Used in Pharmaceutical Research and Development:
H-Phe(2-Me)-OH.HCl is used as a building block for [peptide synthesis] in the creation of novel pharmaceuticals and biologically active molecules, leveraging its capacity to influence the biological properties of these compounds.
Used in Drug Design:
H-Phe(2-Me)-OH.HCl is utilized as a key component in [drug design and discovery], contributing to the development of new therapeutic agents by providing a structural modification that can alter the activity and selectivity of drug candidates.

Upstream product

• 1448452-64-9 1-(hydroxymethyl)-4-(o-tolyl)azetidin-2-one 
• 83725-15-9 4-(o-tolyl)azetidin-2-one 
• 736131-48-9 (S)-3-amino-3-(2-methylphenyl)propionic acid 
• 611-15-4 1-methyl-2-vinyl-benzene 
• 1448452-65-0 (S)-1-(hydroxymethyl)-4-(o-tolyl)azetidin-2-one 
• 21464-57-3 ethyl 3-amino-3-(o-tolyl)propanoate 

Relevant academic research and scientific papers

The N-Hydroxymethyl Group as a Traceless Activating Group for the CAL-B-Catalysed Ring Cleavage of β-Lactams: A Type of Two-Step Cascade Reaction

An efficient enzymatic two-step cascade procedure has been devised for rapid access to diverse amino acids from N-hydroxymethyl-β-lactams; representative amino acids include the antifungal agent cispentacin, intermediates for the taxol side-chain, and assorted cathepsin inhibitors. When CAL-B-catalysed hydrolyses of racemic N-hydroxymethyl-β-lactams were performed with H2O (0.5 equiv.) in iPr2O at 60 °C, relatively quick (vs. non-activated counterparts) and enantioselective (E > 200) ring cleavage reactions took place. As the ring-opened amino acids formed, the hydroxymethyl group, as a traceless activating group, underwent spontaneous in situ degradation. Consequently, the desired β-amino acid and unreacted N-hydroxymethyl-β-lactam enantiomers (ee > 95 %) were formed. The formation of polymers, induced by liberation of formaldehyde, was successfully restricted by the addition of benzylamine as a capture agent, to the enzymatic reactions. An efficient enzymatic two-step cascade procedure was devised for CAL-B-catalysed hydrolysis of racemic N-hydroxymethyl-β-lactams. Conditions in which the hydroxymethyl group serves as a traceless activating group (E > 200), giving desired β-amino acid along with unreacted starting lactam enantiomers (ee > 95 %) were identified; polymerization was controlled by addition benzylamine addition.

Enzymatic preparation of (S)-3-amino-3-(o-tolyl)propanoic acid, a key intermediate for the construction of Cathepsin inhibitors

Enantiomerically pure (S)-3-amino-3-(o-tolyl)propanoic acid [(S)-6], identified as the preferred enantiomeric form for the construction of novel β-amino acid derivatives as inhibitors of Cathepsin, was prepared through both indirect and direct enzymatic strategies. Resolution of hydroxymethylated β-lactam (±)-1 through Burkholderia cepacia lipase PSIM-catalysed R-selective butyrylation (E > 200) was first carried out in t-BuOMe. Treatment of the unreacted (S)-1 with 18% HCl then furnished the desired (S)-6·HCl. Next, Candida antarctica lipase B catalysed the ring cleavage of racemic 4-(o-tolyl)azetidin-2-one [(±)-2] with excellent R enantioselectivity (E > 200), either in t-BuOMe with added H2O as nucleophile or in H2O at 60 C. Hydrolysis of the less reactive β-lactam enantiomer [(S)-2] with 18% HCl afforded (S)-6·HCl. A direct enzymatic route to enantiomeric (S)-6 was finally optimized through the lipase PSIM-catalysed S-enantioselective (E > 200) hydrolysis of racemic ethyl 3-amino-3-(o-tolyl)propanoate [(±)-3] in t-BuOMe with added H 2O at 45 C or in H2O at 3 C.