92136-43-1Relevant academic research and scientific papers
Aryne-mediated [2,3]-sigmatropic rearrangement of tertiary 2,3-allenylamines bearing an electron-withdrawing group at the α-position
Han, Lu,Tian, Shi-Kai,Xie, Dong,Zhang, Xue-Ting
, p. 5353 - 5357 (2021)
An unprecedented [2,3]-sigmatropic rearrangement reaction of quaternary 2,3-allenylammonium ylides, generatedin situfrom tertiary 2,3-allenylamines and arynes, has been established. With 2-(trimethylsilyl)aryl triflates as aryne precursors, a range of tertiary 2,3-allenylamines bearing an electron-withdrawing group at the α-position smoothly participated in the aryne-mediated [2,3]-sigmatropic rearrangement at room temperature, delivering structurally diverse 2-vinylallyamines or 1-amino-1,3-dienes in moderate to excellent yields. The reaction proceeds in the absence of strong bases and transition metals, is compatible with moisture and air, and tolerates a wide variety of functional groups.
Selective inhibition of bovine plasma amine oxidase by homopropargylamine, a new inactivator motif
Qiao, Chunhua,Jeon, Heung-Bae,Sayre, Lawrence M.
, p. 8038 - 8045 (2007/10/03)
Propargylic and activated allylic amines are known to inactivate the quinone-dependent plasma amine oxidases, possibly through active-site modification by the α,β-unsaturated aldehyde turnover products. Although homopropargylamine (1-amino-3-butyne, 1) is a nonobvious candidate as a mechanism-based inhibitor, 1 was found to be an unusually potent time- and concentration-dependent irreversible inactivator of bovine plasma amine oxidase (BPAO), exhibiting a 30 min IC50 of 2.9 μM at 30 °C ([BPAO] = 1.2 μM). Preserved cofactor redox activity of the denatured inactivated enzyme indicates that inactivation by 1 involves either a cofactor modification that reverses upon enzyme denaturation or a modification of an active-site residue. Because inactivation by 1 may involve enzyme alkylation by the reactive 2,3-butadienal (3) tautomer of the 3-butynal turnover product of 1, aldehyde 3 was prepared and was found to inactivate BPAO, but only at high concentration. In addition, whereas inhibition by 3 was blunted by the presence of mercaptoethanol, no such protection was observed against 1. The amine whose turnover should lead directly to 3 was prepared (1-amino-2,3-butadiene, 4) and was found to be an even more potent inactivator of BPAO than 1, exhibiting a 5 min IC50 of 1.25 μM. Rat liver mitochondrial monoamine oxidase was also inactivated by 4, as expected, but only very weakly by 1. Potential mechanisms explaining the selective inhibition of BPAO by 1 are discussed.
Method of potentiating cell-mediated immunity utilizing polyamine derivatives
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, (2008/06/13)
This invention relates to a method of potentiating cell-mediated immunity which comprises administering to a patient a cell-mediated immunity potentiating amount of a compound of the formula: or a pharmaceutically acceptable salt thereof, wherein m is
GENERAL SYNTHETIC ACCESS TO α-ALLENYL AMINES AND α-ALLENYL-α-AMINOACIDS AS POTENTIAL ENZYME ACTIVATED IRREVERSIBLE INHIBITORS OF PLP DEPENDENT ENZYMES
Casara, Patrick,Jund, Karin,Bey, Philippe
, p. 1891 - 1894 (2007/10/02)
The entitled allene derivatives have been prepared from the parent α-ethynyl amines and α-amino acids.The corresponding derivative of GABA, putrescine and phenylalanine have been found to be irreversible and time dependent inhibitors of GABA-T, ODC and ba
