25580-87-4

Upstream product

• 186581-53-3 diazomethane 
• 1947-00-8 6-(benzyloxycarbonylamino)hexanoic acid 
• 67-56-1 methanol 
• 1926-80-3 methyl 6-aminocaproate hydrochloride 
• 501-53-1 benzyl chloroformate 
• 60-32-2 6-aminohexanoic acid 
• 62252-26-0 JLK 6 

Downstream Products

• 82830-85-1 methyl 6-{[(benzyloxy)carbonyl]amino}-2-diazohexanoate 
• 98648-05-6 6-oxo-hexyl-carbamic acid benzyl ester 
• 17996-12-2 N-benzyloxycarbonyl-6-amino-1-hexanol 

Relevant academic research and scientific papers

Further characterization of a putative serine protease contributing to the γ-secretase cleavage of β-amyloid precursor protein

The 3-alkoxy-7-amino-4-chloro-isocoumarins JLK-6 and JLK-2 have been shown to markedly reduce the production of Amyloid β-peptide (Aβ) by Amyloid-β Precursor Protein (APP) expressing HEK293 cells by affecting the γ-secretase cleavage of APP, with no effect on the cleavage of the Notch receptor. This suggested that these compounds do not directly inhibit the presenilin-dependent γ-secretase complex but more likely interfere with an upstream target involved in γ-secretase-associated pathway. The mechanism of action of these compounds is unknown and there are high fundamental and therapeutical interests to unravel their target. Isocoumarin compounds were previously shown to behave as potent mechanism-based irreversible inhibitors of serine proteases, suggesting that the JLK-directed target could belong to such enzyme family. To get further insight into structure-activity relationships and to develop more potent isocoumarin derivatives, we have synthesized and evaluated a series of isocoumarin analogues with modifications at positions 3, 4 and 7. In particular, the 7-amino group was substituted with either acyl, urethane, alkyl or aryl groups, which could represent additional interaction sites. Altogether, the results highlighted the essential integrity of the 3-alkoxy-7-amino-4-chloro-isocoumarin scaffold for Aβ-lowering activity and supported the involvement of a serine protease, or may be more generally, a serine hydrolase. The newly reported 7-N-alkyl series produced the most active compounds with an IC50 between 10 and 30 μM. Finally, we also explored peptide boronates, a series of reversible serine protease inhibitors, previously shown to also lower cellular Aβ production. The presented data suggested they could act on the same target or interfere with the same pathway as isocoumarins derivatives.

TRISUBSTITUTED AMINE COMPOUND

The present invention relates to a compound of the general formula (1): wherein, Y is a methylene group, and the like; A is an optionally substituted heterocyclic group, and the like; B is an optionally substituted heterocyclic group, and the like; R1 is an optionally substituted alkyl group, wherein the alkyl group further may optionally be substituted by an optionally substituted homocyclic group, and the like; and R2 is an optionally substituted amino group, and the like; or a pharmaceutically acceptable derivative thereof, which has an inhibitory activity against cholesteryl ester transfer protein (CETP), thereby being useful for prophylaxis and/or treatment of arteriosclerotic diseases, hyperlipemia or dyslipidemia, and the like.

Aryl sulfonamides and sulfamide derivatives and uses thereof

This invention is directed to novel aryl sulfonamide and sulfamide compounds which bind selectively to and inhibit the activity of the human Y5 receptor. This invention is also related to uses of these compounds for the treatment of feeding disorders such

Asymmetric catalysis of intramolecular N-H insertion reactions of α-diazocarbonyls

Intramolecular N-H insertion reactions of α-diazocarbonyl substrates are catalysed by rhodium(II) carboxylates with catalyst-dependent competition with C-H insertion and β-elimination; asymmetric N-H insertion leading to a pipecolic acid derivative with ee up to 45% is achieved using chiral catalysts.