78331-03-0

Upstream product

• 23680-31-1 BOC-O-benzyl-L-serine 
• 66866-45-3 C₂₀H₂₉NO₇ 
• 2592-95-2 benzotriazol-1-ol 
• 13650-73-2 2,5-dioxopyrrolidin-1-yl O-benzyl-N-t-butoxycarbonyl-L-serinate 
• 620-05-3 iodomethylbenzene 
• 3262-72-4 (S)-N-(tert-butoxycarbonyl)serine 

Downstream Products

• 67320-80-3 (S)-2-Amino-3-benzyloxy-propionamide 
• 244778-26-5 N-tert-butyloxycarbonyl-O-benzyl serine nitrile 
• 244778-31-2 (3-benzyloxy-2-tert-butoxycarbonylamino-propyl)-carbamic acid 4-nitro-phenyl ester 
• 328547-44-0 ((R)-2-amino-1-benzyloxymethyl-ethyl)-carbamic acid tert-butyl ester 
• 645394-47-4 (R)-2-Amino-3-benzyloxy-propionitrile 

Relevant academic research and scientific papers

Molecular Design and Synthesis of a Planar Telomestatin Analogue

Hypothetical macrocycles containing eight fused oxazole units would be logical planar analogues of telomestatin, but DFT calculations suggest the presence of excessive macrocyclic ring strain in such molecules that could complicate their synthesis and/or

DIPEPTIDE MIMETICS OF NGF AND BDNF NEUROTROPHINS

The invention relates to compounds having either agonist or antagonist activities for the neurotrophins NGF and BDNF and represented by monomeric or dimeric substituted dipeptides that are analogs of the exposed portions of loop 1 or loop 4 regions of these neurotrophins near or at a beta-turn of the respective loop. N-acylated substituents of these dipeptides are biostereoisomers of the amino acid residues preceding these dipeptide sequences in the neurotrophin primary structure. The dimeric structure is produced advantageously by using hexatnethylenediaanine to which dipeptides are attached via their carboxyl groups. The claimed compounds displayed neuroprotective and differentiation-inducing activities in cellular models and enhanced the amount of phosphorylated tyrosine kinase A and the heat shock proteins Hsp32 and Hsp70 in the concentration range of 10 -9 to 10 -5 M. They also displayed neuroprotective, anti-parkinsonian, anti-stroke, anti-ischemic, anti-depressant and anti-amnestic activities in animal models and were active in experimental models of Alzheimer's disease. These in vivo effects of the claimed compounds are displayed in the dose range of 0.01 to 10 mg/kg when administered intraperitoneally.

Amidation of carboxylic acids via the mixed carbonic carboxylic anhydrides and its application to synthesis of antidepressant (1S,2R)-tranylcypromine

Primary amidations of carboxylic acids 1 or 3 with NH4Cl in the presence of ClCO2Et and Et3N were developed to afford the corresponding primary amides in 22% to quantitative yields. Additionally, we have applied the amidation to the preparation of various amides containing hydroxamic acids and achieved the synthesis of (1S,2R)-tranylcypromine as an antidepressant medicine via Lossen rearrangement.

Isoselenocyanates derived from Boc/Z-amino acids: Synthesis, isolation, characterization, and application to the efficient synthesis of unsymmetrical selenoureas and selenoureidopeptidomimetics

Isoselenocyanates derived from Boc/Z-amino acids are prepared by the reaction of the corresponding isonitriles with selenium powder in presence of triethylamine at reflux. The utility of these new classes of isoselenocyanates in the preparation of selenoureidodipeptidomimetics possessing both amino as well as carboxy termini has been accomplished. The 1H NMR analysis confirmed that the protocol involving the conversion of isonitriles to isoselenocyanates and their use as coupling agents in assembling selenoureido derivatives is free from racemization.

Synthesis of Boc-amino tetrazoles derived from α-amino acids

A simple route for the synthesis of Boc-protected tetrazole analogs of amino acids starting from Nα-Boc amino acids has been described. The [2 + 3] cycloaddition of Boc-α-amino nitrile and sodium azide in the presence of a catalytic amount of zinc bromide yielded the desired tetrazoles in good yields and purity. All the compounds obtained have been characterized by 1H and 13C-NMR and mass spectral studies. Copyright Taylor & Francis Group, LLC.

Identification of a novel class of succinyl-nitrile-based Cathepsin S inhibitors

The synthesis and in vitro activities of a series of succinyl-nitrile-based inhibitors of Cathepsin S are described. Several members of this class show nanomolar inhibition of the target enzyme as well as cellular potency. The inhibitors displaying the greatest potency contain N-alkyl substituted piperidine and pyrrolidine rings spiro-fused to the α-carbon of the P1 residue.

A reversible cysteines protease aminonitrile effective as a new

Disclosed are novel nitrile compounds of formula (I) further defined herein, which compounds are useful as reversible inhibitors of cysteine proteases such as cathepsin K, S, F, L and B. These compounds are useful for treating diseases and pathological co

Novel nitriles useful as reversible inhibitors of cysteine proteases

Disclosed are novel nitrile compounds of formula (I) further defined herein, which compounds are useful as reversible inhibitors of cysteine proteases such as cathepsin K, S, F, L and B. These compounds are useful for treating diseases and pathological co

Design and synthesis of dipeptide nitriles as reversible and potent cathepsin S inhibitors

The specificity of the immune response relies on processing of foreign proteins and presentation of antigenic peptides at the cell surface. Inhibition of antigen presentation, and the subsequent activation of T-cells, should, in theory, modulate the immune response. The cysteine protease Cathepsin S performs a fundamental step in antigen presentation and therefore represents an attractive target for inhibition. Herein, we report a series of potent and reversible Cathepsin S inhibitors based on dipeptide nitriles. These inhibitors show nanomolar inhibition of the target enzyme as well as cellular potency in a human B cell line. The first X-ray crystal structure of a reversible inhibitor cocrystallized with Cathepsin S is also reported.

Identification of dipeptidyl nitriles as potent and selective inhibitors of cathepsin B through structure-based drug design

Cathepsin B is a member of the papain superfamily of cysteine proteases and has been implicated in the pathology of numerous diseases, including arthritis and cancer. As part of an effort to identify potent, reversible inhibitors of this protease, we examined a series of dipeptidyl nitriles, starting with the previously reported Cbz-Phe-NH-CH2CN (19, IC50 = 62 μM). High-resolution X-ray crystallographic data and molecular modeling were used to optimize the P1, P2, and P3 substituents of this template. Cathepsin B is unique in its class in that it contains a carboxylate recognition site in the S2′ pocket of the active site. Inhibitor potency and selectivity were enhanced by tethering a carboxylate functionality from the carbon α to the nitrile to interact with this region of the enzyme. This resulted in the identification of compound 10, a 7 nM inhibitor of cathepsin B, with excellent selectivity over other cysteine cathepsins.