60758-60-3Relevant academic research and scientific papers
DUAL FUNCTIONING IONIC LIQUIDS AND SALTS THEREOF
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Page/Page column 112, (2010/08/04)
Disclosed herein are ionic liquid compositions comprising active pharmaceutical, biological, and nutritional compounds, and methods of use. Further disclosed are compositions of matter including liquid ion pairs alone or in solution and their use; compositions of ionic liquids that are 'solvated,' for example, 'hydrated' and their uses.
Functional alcohol releasing substance
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, (2008/06/13)
This invention discloses a substance which is a betaine ester of a functional alcohol that has an amido bond in its molecule and releases the functional alcohol.
Betaine esters for delivery of alcohols
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, (2008/06/13)
The invention concerns compositions comprising a compound of general formula selected from: Said compositions show an excellent deposition to a surface followed by delayed release of the R-group. More in particular, the invention relates to betaine-ester quaternary ammonium derivatives having an odoriferous alcohol as releasable R-group such as geraniol.
Photoactive analogs of farnesyl pyrophosphate containing benzoylbenzoate esters: Synthesis and application to photoaffinity labeling of yeast protein farnesyltransferase
Gaon, Igor,Turek, Tammy C.,Weller, Valerie A.,Edelstein, Rebecca L.,Singh, Satinder K.,Distefano, Mark D.
, p. 7738 - 7745 (2007/10/03)
Farnesyl pyrophosphate (FPP) is involved in a large number of cellular processes including the prenylation of transforming mutants of Ras proteins implicated in cancer. Photoactive analogs could provide useful information about enzyme active sites that bind farnesyl pyrophosphate; however, the availability of such compounds is extremely limited. Molecules that incorporate benzophenone moieties are attractive photoaffinity labeling reagents because of their useful photochemical properties. Here, the syntheses of two compounds, 3a and 3b, containing para- and meta-substituted benzoylbenzoates are described. Compounds 3a and 3b are competitive inhibitors (with respect to FPP) of yeast protein farnesyltransferase (PFTase) with K(i) values of 910 and 380 nM, respectively. Both compounds inactivate PFTase upon photolysis, resulting in as much as 44% inactivation of enzyme activity. Photolysis of PFTase in the presence of [32P]3a or of [32P]3b results in preferential labeling of the β subunit, suggesting that this subunit is involved in prenyl group recognition. These compounds should be valuable tools for studying enzymes that utilize FPP as a substrate.
