96042-15-8Relevant academic research and scientific papers
DIPEPTIDE ANALOGS AS COAGULATION FACTOR INHIBITORS
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Page/Page column 131-132, (2009/01/23)
Disclosed are novel dipeptide analogs compounds of Formula (I), (II) or (III) or a stereoisomer, a tautomer, a pharmaceutically acceptable salt, a solvate, or a prodrug thereof, which are inhibitors of factor XIa and/or plasma kallikrein, compositions containing them, and methods of using them, for example, for the treatment or prophylaxis of thrombotic diseases.
Trapping of the Intermediate Formed in the E1cB Hydrolysis of Some Alkyl and Aryl N-(4-Nitrophenyl)carbamates in a Hydroxy Functionalized Micelle
Broxton, Trevor J.
, p. 77 - 83 (2007/10/02)
The basic hydrolyses of some alkyl and aryl N-(4-nitrophenyl)carbamates in the presence of micelles of cetyl(2-hydroxyethyl)dimethylammonium bromide (chedab) were studied.For compounds which react by the BAC2 mechanism, very similar results were obtained in cetyltrimethylammonium bromide (ctab) and in chedab micelles.However, for compounds which react by the E1cB mechanism, the intermediate p-nitrophenyl isocyanate was trapped by the hydroxy group of the functional micelle to form a new carbamate directly bound to the detergent molecules of the micelle.It was shownthat this new carbamate decomposed by a BAC2 mechanism. p-Nitrophenyl isocyanate added to an alkaline solution of chedab gave N-(4-nitrophenyl)carbamate ion.Thus, the isocyanate has to be generated within the micelle for trapping to occur.The rate of reaction of p-nitrophenyl isocyanate with OH-/H2O is faster than the rate of solubilization within the micelle.
