ol-135 and oleylamide

ol-135 has been researched along with oleylamide* in 1 studies

Other Studies

1 other study(ies) available for ol-135 and oleylamide

Article	Year
Potent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolase. Journal of medicinal chemistry, 2007, Mar-08, Volume: 50, Issue:5 A study of the structure-activity relationships (SAR) of 2f (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed, targeting the 5-position of the oxazole. Examination of a series of substituted benzene derivatives (12-14) revealed that the optimal position for substitution was the meta-position with selected members approaching or exceeding the potency of 2f. Concurrent with these studies, the effect of substitution on the pyridine ring of 2f was also examined. A series of small, nonaromatic C5-substituents was also explored and revealed that the K(i) follows a well-defined correlation with the Hammett sigma(p) constant (rho = 3.01, R2 = 0.91) in which electron-withdrawing substituents enhance potency, leading to inhibitors with K(i)s as low as 400 pM (20n). Proteomic-wide screening of the inhibitors revealed that most are exquisitely selective for FAAH over all other mammalian proteases, reversing the 100-fold preference of 20a (C5 substituent = H) for the enzyme TGH. Topics: Amidohydrolases; Animals; Arachidonic Acids; Benzene Derivatives; Chlorocebus aethiops; COS Cells; Endocannabinoids; Humans; Oleic Acids; Oxazoles; Polyunsaturated Alkamides; Proteomics; Rats; Recombinant Proteins; Structure-Activity Relationship	2007

Article

Year

Potent and selective alpha-ketoheterocycle-based inhibitors of the anandamide and oleamide catabolizing enzyme, fatty acid amide hydrolase.

Journal of medicinal chemistry, 2007, Mar-08, Volume: 50, Issue:5

A study of the structure-activity relationships (SAR) of 2f (OL-135), a potent inhibitor of fatty acid amide hydrolase (FAAH), is detailed, targeting the 5-position of the oxazole. Examination of a series of substituted benzene derivatives (12-14) revealed that the optimal position for substitution was the meta-position with selected members approaching or exceeding the potency of 2f. Concurrent with these studies, the effect of substitution on the pyridine ring of 2f was also examined. A series of small, nonaromatic C5-substituents was also explored and revealed that the K(i) follows a well-defined correlation with the Hammett sigma(p) constant (rho = 3.01, R2 = 0.91) in which electron-withdrawing substituents enhance potency, leading to inhibitors with K(i)s as low as 400 pM (20n). Proteomic-wide screening of the inhibitors revealed that most are exquisitely selective for FAAH over all other mammalian proteases, reversing the 100-fold preference of 20a (C5 substituent = H) for the enzyme TGH.

Topics: Amidohydrolases; Animals; Arachidonic Acids; Benzene Derivatives; Chlorocebus aethiops; COS Cells; Endocannabinoids; Humans; Oleic Acids; Oxazoles; Polyunsaturated Alkamides; Proteomics; Rats; Recombinant Proteins; Structure-Activity Relationship

2007