1041867-85-9Relevant academic research and scientific papers
Preparation and synthetic applications of N-(α,β-unsaturated acyl)-α-amino acid derivatives
Katritzky, Alan R.,Gyanda, Reena,Meher, Nabin K.,Song, Yuming
experimental part, p. 1249 - 1259 (2010/10/03)
N-(α,β-Unsaturated acyl)-α-amino acids, amides and esters are structural motifs of many biologically active natural products. An alternate and advantageous approach for the synthesis of N-(α,β-unsaturated acyl)-α-amino acid derivatives is developed via ac
Cinnamoyl inhibitors of tissue transglutaminase
Pardin, Christophe,Pelletier, Joelle N.,Lubell, William D.,Keillor, Jeffrey W.
, p. 5766 - 5775 (2008/12/22)
(Figure Presented) Transglutaminases (TGases) catalyze the intermolecular cross-linking of certain proteins and tissue TGases (TG2) are involved in diverse biological processes. Unregulated, high TGase activities have been implicated in several physiological disorders, but few reversible inhibitors of TG2 have been reported. Herein, we report the synthesis of a series of novel trans-cinammoyl derivatives, discovered to be potent inhibitors of guinea pig liver transglutaminase. The most effective inhibitors evaluated can be sorted into two subclasses: substituted cinnamoyl benzotriazolyl amides and the 3-(substituted cinnamoyl)pyridines, referred to more commonly as azachalcones. Kinetic evaluation of both of these subclasses revealed that they display reversible inhibition and are competitive with acyl donor TGase substrates at IC50 values as low as 18 μM. An analysis of structure - activity relationships within these series of inhibitors permitted the identification of potentially important binding interactions. Further testing of some of the most potent inhibitors demonstrated their selectivity for TG2 and their potential for further development.
