27588-56-3

Upstream product

• 2067-33-6 5-bromopentanoic acid 
• 100-53-8 phenylmethanethiol 
• 100-44-7 benzyl chloride 

Downstream Products

• 5331-36-2 methyl 3-(benzylthio)propanoate 
• 73975-55-0 benzyl 2-methoxycarbonylethyl sulphoxide 
• 189103-48-8 methyl 5-(benzylsulfanyl)pentanoate 
• 1962-44-3 4-(benzylthio)pentan-1-ol 
• 1313593-29-1 C₁₅H₂₅NOS 
• 1313593-28-0 C₁₅H₂₁NOS 
• 945413-88-7 5-(benzylthio)-1-(5-(pyridin-2-yl)oxazol-2-yl)pentan-1-one 
• 446874-28-8 C₁₂H₁₅OSCl 

Relevant academic research and scientific papers

A synthesis of C-glycosidic multivalent mannosides suitable for divergent functionalized conjugation

Divergent synthesis of two novel C-glycosidic multivalent mannosides derived from a common trivalent C-mannosyl carboxylate-terminated intermediate is described. This illustrates synthesis of multivalent C-glycosidic architectures bearing variable extende

TRICYCLIC INHIBITORS OF FATTY ACID AMIDE HYDROLASE

A series of substituted oxazole compounds having an alpha keto side chain at the 2 position and an aromatic, heteroaromatic or heterocycle substituent at the 5 position are disclosed. These compounds exhibit inhibition of fatty acid amid hydrolase and are useful for treatment of malconditions involving that enzyme.

Structure-activity relationships of α-ketooxazole inhibitors of fatty acid amide hydrolase

A systematic study of the structure-activity relationships of 2b (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed targeting the C2 acyl side chain. A series of aryl replacements or substituents for the terminal phenyl group provided effective inhibitors (e.g., 5c, aryl = 1-napthyl, K, - 2.6 nM), with 5hh (aryl -3-ClPh, Ki = 900 pM) being 5-fold more potent than 2b. Conformationally restricted C2 side chains were examined, and many provided exceptionally potent inhibitors, of which 11j (ethylbiphenyl side chain) was established to be a 750 pM inhibitor. A systematic series of heteroatoms (O, NMe, S), electron-withdrawing groups (SO, SO2), and amides positioned within and hydroxyl substitutions on the linking side chain were investigated, which typically led to a loss in potency. The most tolerant positions provided effective inhibitors (12p, 6-position S, Ki = 3 nM, or 13d, 2-position OH, Ki = 8 nM) comparable in potency to 2b. Proteome-wide screening of selected inhibitors from the systematic series of >100 candidates prepared revealed that they are selective for FAAH over all other mammalian serine proteases.

Biotransformation of organic sulfides - VIII. A predictive model for sulfoxidation by Helminthosporium species NRRL 4671

The fungus Helminthosporium species NRRL 4671 converts a wide range of prochiral sulfides to the corresponding chiral sulfoxides, the majority of which have (S) configuration at sulfur. The formation of a series of chiral cyclopentyl alkyl, cyclohexyl alkyl, benzyl alkyl, and methyl alkyl sulfoxides by biotransformation of the corresponding sulfides using Helminthosporium species is described. The analysis of over 90 such biotransformations has resulted in the development of a model based on restrictive-space descriptors that has been used to rationalize these reactions, and that is proposed as a predictor of the outcome of Helminthosporium-catalyzed sulfoxidations.