16536-62-2Relevant articles and documents
Acylation of cellulose in a novel solvent system: Solution of dibenzyldimethylammonium fluoride in DMSO
Casarano, Romeu,Pires, Paulo A.R.,El Seoud, Omar A.
, p. 444 - 450 (2014)
A novel electrolyte, dibenzyldimethylammonium fluoride has been obtained essentially anhydrous (BMAF-0.1H2O) by a simple route. Its thermal stability, relative to tetra(1-butyl)ammonium fluoride trihydrate (TBAF3H 2O) has been demons
Apparent molar volumes of benzyltrimethylammonium bromide and its homologs in aqueous solution at 15, 25, and 35°C
Tutaj,Gonzalez-Perez,Czapkiewicz,Del Castillo,Rodriguez
, p. 1101 - 1109 (2001)
Apparent molar volumes at infinite dilution of benzyltrimethylammonium bromide and its butyl and hexyl homologs at 15, 25, and 35°C and of dibenzyldimethylammonium bromide at 25°C in aqueous solution were estimated from density measurements. The additivity rule for the contribution of the methylene groups to the apparent molar volumes was found to be obeyed within a broad range of homologs, which covers the parent salt and the dodecyldimethylbenzylammonium bromide. The volumetric contribution of the phenylene (-C6H4-) group was estimated to be 61 cm3-mol-1 at 25°C. A value of - 16.9 ± 0.3 cm3-mol-1 was suggested for the volumetric contribution of the N+ fragment to the apparent molar volume of alkylbenzyldimethylammonium salts.
Preparation, in vitro screening and molecular modelling of mono-quaternary compounds related to the selective acetylcholinesterase inhibitor BW284c51
Benek, Ondrej,Musilek, Kamil,Horova, Anna,Dohnal, Vlastimil,Dolezal, Rafael,Kuca, Kamil
, p. 21 - 29 (2015/04/14)
This paper describes preparation and in vitro evaluation of 19 compounds related to the selective experimental cholinesterase inhibitor BW284c51. The novel compounds were prepared as fragments of parent molecule BW284c51 and evaluated on the model of human recombinant acetylcholinesterase and human plasmatic butyrylcholinesterase. The IC50 values of the prepared compounds were compared to the parent molecule BW284c51. None of the compounds was superior to the parent drug, but two BW284c51 fragments showed promising hAChE inhibition in μM scale and improved selectivity. These two fragments were further subjected to the molecular modelling study and their enzyme interactions were rationalized. The structure-activity relationship of the prepared series was stated.
