10369-82-1Relevant articles and documents
Simple and efficient method for acetylation of alcohols, phenols, amines, and thiols using anhydrous NiCl2 under solvent-free conditions
Meshram, Gangadhar,Patil, Vishvanath D.
, p. 4384 - 4395 (2009)
Solvent-free acetylation of alcohols, phenols, amines, and thiols with acetic anhydride (Ac2O) in the presence of 0.1mol% (13mg) anhydrous NiCl2, an inexpensive and easily available catalyst, is described. Excellent yields, short reaction time, and mild reaction conditions are important features of this method.
Dual-Channel Enzymatic Inhibition Measurement (DEIM) Coupling Isotope Substrate via Matrix-Assisted Laser Desorption/Ionization Time of Flight Mass Spectrometry
Tao, Min,Zhang, Li,Guo, Yinlong
, p. 2427 - 2435 (2018)
A novel dual-channel enzymatic inhibition measurement (DEIM) method was developed to improve the repeatability with light/heavy isotope substrates, producing reliable relative standard deviations ( 3%) by employing acetylcholinesterase (AChE) as the model enzyme. The matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) was adapted for enzyme-inhibited method due to its good salt-tolerance and high throughput; meanwhile, dual-channel enzymatic reactions were performed to improve the repeatability of each well. The acetylcholinesterase inhibition measurement was conducted by mixing the quenched enzyme reaction solution of blank group (with heavy isotope as substrate) and experimental group (with light isotope as substrate), of which the inhibition rate might be affected by isotope effects. Hence, inverse study and Km measurement were implemented to validate the method. The inverse study shows similar inhibition rate (68.9 and 70.3%) and the Km of isotope substrates are analogous (0.139 and 0.135?mM), which demonstrated that the novel method is feasible to AChE inhibition measurement. Finally, the method was applied to herb extracts, half of which exhibit inhibition to AChE. The precise dual-channel enzymatic inhibition measurement (DEIM) method could be regarded as a promising approach to potential enzyme inhibitor screening. [Figure not available: see fulltext.].
Stereospecific Palladium-Promoted Oxyamination of Alkenes
Baeckvall, Jan E.,Bjoerkman, Eva E.
, p. 2893 - 2898 (2007/10/02)
A method for direct oxyamination of olefins to vicinal amino alcohol derivatives is described. The reaction proceeds via an aminopalladation-oxidation sequence.Terminal olefins give good yields (60-80percent) whereas internal olefins give lower yields (20-60percent).The oxyamination reaction is stereospecific as shown by reaction of (Z)- and (E)-2-butene and (E)-1-deuterio-1-decene and proceeds by overall cis stereochemistry.The stereochemical outcome is a result of a trans aminopalladation followed by an oxidative cleavage of the palladium carbon bond with inversion of configuration at carbon.Oxidation of the organopalladium ? complex to give an oxidized palladium intermediate, which could be a Pd(IV) intermediate, followed by SN2-type nucleophilic displacement of palladium is the most likely mechanism for the oxidative cleavage reaction.