137278-22-9

Upstream product

• 1826-67-1 vinyl magnesium bromide 
• 87694-53-9 Boc-Phe-OH N,O-dimethyl hydroxamate 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 3536-96-7 vinylmagnesium chloride 

Downstream Products

• 160002-17-5 ((1S,2R)-1-Benzyl-2-hydroxy-2-vinyl-pent-4-enyl)-carbamic acid tert-butyl ester 
• 160002-07-3 ((1S,2S)-1-Benzyl-2-hydroxy-2-vinyl-pent-4-enyl)-carbamic acid tert-butyl ester 
• 99113-30-1 ((1S,2R)-1-benzyl-2-hydroxybut-3-enyl)carbamic acid tert-butyl ester 
• 99113-28-7 (3S,4S)-5-[(tert-butoxycarbonyl)amino]-3-hydroxy-5-phenyl-1-pentene 
• 181047-29-0 (S)-tert-butyl (3,3-difluoro-1-phenylpent-4-en-2-yl)carbamate 
• 99113-28-7 4-<<(tert-butyloxy)carbonyl>amino>-3-hydroxy-5-phenyl-1-pentene 

Relevant academic research and scientific papers

Synthesis and biological evaluations of novel endomorphin analogues containing α-hydroxy-β-phenylalanine (AHPBA) displaying mixed μ/δ opioid receptor agonist and δ opioid receptor antagonist activities

A novel series of endomorphin-1 (EM-1) and endomorphin-2 (EM-2) analogues was synthesized, incorporating chiral α-hydroxy-β-phenylalanine (AHPBA), and/or Dmt1-Tic2 at different positions. Pharmacological activity and metabolic stabil

Phenylalanine-based inactivator of akt kinase: Design, synthesis, and biological evaluation

Strategies to inhibit kinases by targeting the substrate binding site offer many advantages, including naturally evolved selectivity filters, but normally suffer from poor potency. In this work we propose a strategy to design and prepare covalent substrate-competitive kinase inhibitors as a method to improve potency. We have chosen AKT as the model kinase for this work. Using the AKT-GSK3β cocrystal structure and a reactive cysteine near the substrate binding site, we have identified phenylalanine (Phe) as an appropriate scaffold for the covalent inactivator portion of these inhibitors. By synthesizing compounds that incorporate cysteine-reactive electrophiles into phenylalanine and testing these compounds as AKT inhibitors, we have identified Boc-Phe-vinyl ketone as a submicromolar inactivator of AKT. We also show that Boc-Phe-vinyl ketone (1) potently inhibits AKT1 and inhibits cell growth in HCT116 and H460 cells nearly as well as AKT inhibitors GSK690693 and MK-2206, (2) is selective for kinases that possess an activation loop cysteine such as AKT, (3) requires the vinyl ketone for inactivation, (4) has inactivation that is time-dependent, and (5) alkylates Cys310 of AKT as shown by mass spectrometry. Identification of Boc-Phe-vinyl ketone as a covalent inactivator of AKT will allow the development of peptide and small-molecule substrate-competitive covalent kinase inhibitors that incorporate additional substrate binding elements to increase selectivity and potency. This proof-of-principle study also provides a basis to apply this strategy to other kinases of the AGC and CAMK families.

Phenylamide and pyridylamide beta-secretase inhibitors for the treatment of alzheimer's disease

The present invention is directed to phenylamide and pyridylamide derivative compounds of which are inhibitors of the beta-secretase enzyme and that are useful in the treatment of diseases in which the beta-secretase enzyme is involved, such as Alzheimer's disease. The invention is also directed to pharmaceutical compositions comprising these compounds and the use of these compounds and compositions in the treatment of such diseases in which the beta-secretase enzyme is involved.

Alpha-hydroxyarylbutanamine inhibitors of aspartyl protease

Acylated α-hydroxyarylbutanamines and related sulfonamides, ureas and carbamates that inhibit aspartyl protease are disclosed, as are methods of treating diseases, particularly HIV, using these compounds. The compounds have the formula: 1A representative

Design and synthesis of novel protease inhibitors. Tripeptide α′,ss′-epoxyketones as nanomolar inactivators of the proteasome

Tripeptide α′,β′-epoxyketones were prepared stereospecifically starting from Boc-[S]-phenylalanine. Diastereomer 5b inhibited the chymotrypsin-like activity of porcine endothelial cell derived proteasome at low nanomolar concentrations.

Inactivation of serine protease, α-chymotrypsin by fluorinated phenylalanine analogues

Fluorinated phenylalanine analogues were found to be slow-binding or reversible competitive inhibitors of α-chymotrypsin. A series of these compounds were designed to inactivate α-chymotrypsin as a result of the formation of hydrogen-bonding between fluorine atom of the inhibitors and the amide protons known as oxy-anion hole in the active-site of serine and cysteine proteases.

A convergent synthesis of novel conformationally restricted HIV-1 protease inhibitors

Conformationally restricted HIV-1 protease inhibitors containing the transition state hydroxyl group in pyrrolidine or piperidine ring systems were synthesized stereoselectively utilizing the inherent stereochemistry of an amino acid derivative. A converg

Process for the preparation of a dipeptide isostere

A process and intermediates useful for the preparation of (E)-alkene dipeptide isosteres are disclosed.