The hydrolysis of epoxides catalyzed by inorganic ammonium salts in water: kinetic evidence for hydrogen bond catalysis

2018 ◽  
Vol 20 (3) ◽  
pp. 1583-1590 ◽  
Author(s):  
B. Nozière ◽  
F. Fache ◽  
A. Maxut ◽  
B. Fenet ◽  
A. Baudouin ◽  
...  

Hydrogen-bond catalysis strongly accelerates the hydrolysis of epoxides in aqueous media, and is likely to be important in natural environments.

1922 ◽  
Vol 5 (2) ◽  
pp. 181-188 ◽  
Author(s):  
M. H. Jacobs

1. It may be shown by means of cells of the flowers of a hybrid Rhododendron which contain a natural indicator, by means of starfish eggs stained with neutral red, and by means of an "artificial cell" in which living frog's skin is employed that increased intracellular alkalinity may be brought about by solutions of a decidedly acid reaction which contain ammonium salts. 2. These results are analogous to those previously obtained with the CO2-bicarbonate system, and depend on the facts: (a) that NH4OH is sufficiently weak as a base to permit a certain degree of hydrolysis of its salts; and (b) that living cells are freely permeable to NH4OH (or NH3?) and not to mineral and many organic acids, and presumably not at least to the same extent to ammonium salts as such.


2020 ◽  
Vol 44 (19) ◽  
pp. 7954-7961
Author(s):  
Sanchita Mondal ◽  
Saikat Kumar Manna ◽  
Sudipta Pathak ◽  
Aritri Ghosh ◽  
Pallab Datta ◽  
...  

A chromogenic and “off–on” fluorogenic chemodosimeter (L) based on a naphthalene–rhodamine B derivative was designed, synthesized and characterized for the selective and sensitive detection of Au3+ ions in mixed acetonitrile aqueous media.


2005 ◽  
Vol 13 (3) ◽  
pp. 223-234
Author(s):  
C. Sanglar ◽  
M. Defay ◽  
H. Waton ◽  
A. Bonhomme ◽  
S. Alamercery ◽  
...  

This work on organic dental composites was undertaken to determine the role of residual reactive methacrylate functions at the end of the photopolymerization cycle, and to investigate the fate of the residual monomers and oligomers in organic (ethanol) and aqueous (water and artificial saliva) media. The results show that all the methacrylate monomers present in dentine migrate into ethanol (about 1% (w/w)). In aqueous media on the other hand, only the most hydrophilic monomer (UDMA) migrates (0.05% (w/w)) into water and 0.03% into artificial saliva (pH = 9). This desorption in the three media is accompanied by the hydrolysis of monomers, leading to the formation of monohydrolyzed urethane dimethacrylate (UDMA) and bis-phenyl glycidyl dimethacrylate (BISGMA); UDMA and BISGMA are completely hydrolyzed in artificial saliva. The alkalinity of the milieu apparently favours the hydrolysis of methacrylate functions.


Molecules ◽  
2020 ◽  
Vol 25 (19) ◽  
pp. 4545
Author(s):  
Nurul Amira Nurul Azman ◽  
Maram B. Alhawarri ◽  
Mira Syahfriena Amir Rawa ◽  
Roza Dianita ◽  
Amirah Mohd Gazzali ◽  
...  

Seventeen methanol extracts from different plant parts of five different Cassia species, including C. timorensis, C. grandis, C. fistula, C. spectabilis, and C. alata were screened against acetylcholinesterase (AChE). C. timorensis extracts were found to exhibit the highest inhibition towards AChE whereby the leaf, stem, and flower methanol extracts showed 94–97% inhibition. As far as we are aware, C. timorensis is one of the least explored Cassia spp. for bioactivity. Further fractionation led to the identification of six compounds, isolated for the first time from C. timorensis: 3-methoxyquercetin (1), benzenepropanoic acid (2), 9,12,15-octadecatrienoic acid (3), β-sitosterol (4), stigmasterol (5), and 1-octadecanol (6). Compound 1 showed moderate inhibition towards AChE (IC50: 83.71 μM), while the other compounds exhibited poor to slightly moderate AChE inhibitory activity. Molecular docking revealed that the methoxy substitution of 1 formed a hydrogen bond with TYR121 at the peripheral anionic site (PAS) and the hydroxyl group at C5 formed a covalent hydrogen bond with ASP72. Additionally, the OH group at the C3′ position formed an interaction with the protein at the acyl pocket (PHE288). This possibly explains the activity of 1 in blocking the entry of acetylcholine (ACh, the neurotransmitter), thus impeding the hydrolysis of ACh.


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