2589-78-8Relevant articles and documents
Alkylated phenol series in lacustrine black shales from the Noerdlinger Ries, southern Germany
Barakat, Assem O.,Baumgart, Susan,Brocks, Peter,Scholz-Boettcher, Barbara M.,Rullkoetter, Juergen
, p. 987 - 994 (2012/11/06)
Several series of alkylated phenols were detected for the first time in the extractable bitumens of organic matter-rich sediments from the Noerdlinger Ries (southern Germany). Most abundant and significant constituents comprise those with n-octadecyl, n-eicosanyl, phytanyl, and iso-pentadecyl and anteiso-pentadecyl substituents. The structures of these compounds are suggested from mass spectrometric and retention time data and coinjection with synthetic standards. Diagenetic alteration of phenolic algal lipids is suggested as a possible way to the formation of these compounds in the Noerdlinger Ries sediments. Copyright
Detergent
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, (2010/04/23)
A detergent including one or more neutral or overbased alkaline earth metal C10 to C40 hydrocarbyl substituted hydroxybenzoates, in which: (i) the one or more neutral or overbased alkaline earth metal C10 to C40 hydrocarbyl substituted hydroxybenzoates is or includes one or more C10 to C40 hydrocarb-1-yl substituted hydroxybenzoates; or, (ii) greater than 50 mole % of the one or more neutral or overbased alkaline earth metal C10 to C40 hydrocarbyl substituted hydroxybenzoates, based on the total number of moles of said C10 to C40 hydrocarbyl substituted hydroxybenzoates, is or includes one or more C10 to C40 hydrocarb-2-yl substituted hydroxybenzoates.
Structure-activity relationship studies of the amide functionality in (p-O-sulfamoyl)-N-alkanoyl tyramines as estrone sulfatase inhibitors
Chu, Guo-Hua,Milano, Shawn,Kluth, Lisa,Rhodes, Michael,Boni, Riccardo,Johnson, David A.,Li, Pui-Kai
, p. 530 - 535 (2007/10/03)
Recently, we reported the synthesis and biochemical studies of a series of (p-O-sulfamoyl)-N-alkanoyl tyramines as nonsteroidal estrone sulfatase inhibitors. One of the most potent inhibitors in this series is (p-O- sulfamoyl)-N-tridecanoyl tyramine 1 with an IC50 value of 61.3 nM. In this study, we synthesized four analogs of 1 (compounds 2-5) to investigate the structure-activity relationships of the amide functionality in (p-O- sulfamoyl)-N-tridecanoyl tyramine. Replacement of the amide functionality in 1 with an ethylene moiety to form the alkyl analog 5 resulted in complete loss of sulfatase inhibitory activity (IC50 of 61.3 nM vs. >20 μM). The keto, hydroxy, and ester analogs (inhibitors 2-4) are 8-15 times less in affinity to the sulfatase than inhibitor 1. However, their inhibitory activities are significantly higher than the alkyl analog 5. The results suggest that the amide functionality is favorable for sulfatase inhibitory activity and that there may be a hydrogen bonding component to the enzyme interaction in this region.