910581-07-6

Upstream product

• 497-25-6 dimethylenecyclourethane 
• 20371-41-9 5-phenylvaleric acid chloride 
• 2270-20-4 5-Phenylpentanoic acid 

Downstream Products

• 1330660-76-8 (S)-3-(2,5-diphenylpentanoyl)oxazolidin-2-one 
• 910581-26-9 3-(2-oxooxazolidine-3-carbonyl)-6-phenyl-N-(trityloxy)hexanamide 
• 910581-41-8 2-(3-phenylpropyl)-N¹-(prop-2-ynyl)-N⁴-(trityloxy)succinamide 
• 910581-33-8 2-(2-oxo-2-(trityloxyamino)ethyl)-5-phenylpentanoic acid 
• 910581-19-0 3-(2-oxooxazolidine-3-carbonyl)-6-phenylhexanoic acid 
• 910581-49-6 N⁴-hydroxy-2-(3-phenylpropyl)-N¹-(prop-2-ynyl)succinamide 

Relevant academic research and scientific papers

Substituted Heterocyclic Derivative, Preparation Method And Use Thereof

The invention provides a compound as shown by Formula I having an enzyme activity which can inhibit endocannabinoid hydrolases NAAA and/or FAAH, or a pharmaceutically acceptable salt, hydrate or solvate thereof, and a preparation method and a use of the compound.

Design, synthesis, and biological evaluation of oxazolidone derivatives as highly potent N-acylethanolamine acid amidase (NAAA) inhibitors

N-Acylethanolamine-hydrolyzing acid amidase (NAAA) is a lysosomal enzyme that catalyzes the hydrolysis of endogenous fatty acid ethanolamides (FAEs), such as N-palmitoylethanolamide (PEA). PEA exhibits anti-inflammatory and analgesic activities by engaging peroxisome proliferator-activated receptor α (PPAR-α). Preventing PEA degradation by inhibition of NAAA has been proposed as a novel strategy for the treatment of inflammation and pain. In the present study, we reported the discovery of the oxazolidone derivative as a novel scaffold for NAAA inhibitors, and studied the structure-activity relationship (SAR) by modification of the side chain and terminal lipophilic substituents. The results showed that the link chain length of C5, straight and saturated linkages were the preferred shape patterns for NAAA inhibition. Several nanomolar NAAA inhibitors were described, including 2f, 3h, 3i and 3j with IC50 values of 270 nM, 150 nM, 100 nM and 190 nM, respectively. Enzymatic degradation studies suggested that 2f inhibited NAAA in a selective, noncompetitive and reversible pattern. Moreover, 2f showed high anti-inflammatory and analgesic activities after systemic and oral administration.

Rapid assembly of matrix metalloprotease inhibitors using click chemistry

A panel of 96 metalloprotease inhibitors was assembled using "click chemistry" by reacting eight zinc-binding hydroxamate warheads with 12 azide building blocks. Screens of the bidentate compounds against representative metalloproteases provided discerning inhibition fingerprints, revealing compounds with low micromolar potency against MMP-7. The relative ease and convenience of the strategy in constructing focused chemical libraries for rapid in situ screening of MMPs is thereby demonstrated.