13317-44-7Relevant articles and documents
Dramatic influence of the nature of the surfactant aggregate on the rate constant for hydrolysis of phosphinate esters in aqueous nematic lyotropic liquid crystals
Ramesh,Labes
, p. 738 - 741 (1988)
The o-iodosobenzoic acid catalyzed hydrolysis of two organophosphinate esters has been studied in the lyotropic nematic phases of myrystyltrimethylammonium bromide in 1-decanol, ammonium bromide, and water. Depending on the concentration of these ingredients, three phases are observed at room temperature consisting of rod-like (N//C), disk-like (N//L), or sphere-like (I) aggregates. There is a three order of magnitude difference in the rate constant for hydrolysis between N//L and N//C phases. The N//L phase serves as a protective environment, preventing the hydrolysis of the ester, whereas the N//C phase allows the reaction to occur rapidly. Based upon infrared evidence, the phosphinate ester is solubilized in the hydrocarbon region of N//L aggregates, but in N// C and I aggregates the solute is nearer the aqueous interface.
Resolution of chiral phosphate, phosphonate, and phosphinate esters by an enantioselective enzyme library
Nowlan, Charity,Li, Yingchun,Hermann, Johannes C.,Evans, Timothy,Carpenter, Joseph,Ghanem, Eman,Shoichet, Brian K.,Raushel, Frank M.
, p. 15892 - 15902 (2007/10/03)
An array of 16 enantiomeric pairs of chiral phosphate, phosphonate, and phosphinate esters was used to establish the breadth of the stereoselective discrimination inherent within the bacterial phosphotriesterase and 15 mutant enzymes. For each substrate,
Phosphorous-containing cysteine and serine protease inhibitors
-
, (2008/06/13)
The present invention is directed to novel phosphorous-containing inhibitors of cysteine or serine proteases. Methods for the use of the protease inhibitors are also described.
