20384-14-9Relevant articles and documents
Stereoselective formal hydroamidation of si-substituted arylacetylenes with DIBAL-H and isocyanates: Synthesis of (E)- And (Z)-α-Silyl-α,β-unsaturated amides
Lee, Yunmi,Jung, Byunghyuck,Lee, Hanseul,Cho, Soohong
, p. 12024 - 12035 (2020/11/10)
An efficient and stereoselective method for the synthesis of (E)- and (Z)-α-silyl-α,β-unsaturated amides and its synthetic applications are presented herein. The solvent-controlled hydroaluminations of Si-substituted alkynes with DIBAL-H generate diastereomerically enriched alkenylaluminum reagents that are directly reacted with isocyanates at ambient temperature to afford α-silyl-α,β-unsaturated amides in high yields with retained stereoselectivity. In particular, this process enables the synthesis of a broad range of (E)-α-silyl-α,β- unsaturated amides, which are the less studied isomers. The synthetic utility of this method is highlighted by its short reaction time, ease of purification, easily accessible substrates and reagents, gram-scale synthesis, and the further transformations of C-Si bonds into C-H, C-X, and C-C bonds.
Cinnamic acid amides from Tribulus terrestris displaying uncompetitive α-glucosidase inhibition
Song, Yeong Hun,Kim, Dae Wook,Curtis-Long, Marcus J.,Park, Chanin,Son, Minky,Kim, Jeong Yoon,Yuk, Heung Joo,Lee, Keun Woo,Park, Ki Hun
, p. 201 - 208 (2016/05/02)
The α-glucosidase inhibitory potential of Tribulus terrestris extracts has been reported but as yet the active ingredients are unknown. This study attempted to isolate the responsible metabolites and elucidate their inhibition mechanism of α-glucosidase. By fractionating T. terristris extracts, three cinnamic acid amide derivatives (1-3) were ascertained to be active components against α-glucosidase. The lead structure, N-trans-coumaroyltyramine 1, showed significant inhibition of α-glucosidase (IC50 Combining double low line 0.42 μM). Moreover, all active compounds displayed uncompetitive inhibition mechanisms that have rarely been reported for α-glucosidase inhibitors. This kinetic behavior was fully demonstrated by showing a decrease of both Km and Vmax, and Kik/Kiv ratio ranging between 1.029 and 1.053. We progressed to study how chemical modifications to the lead structure 1 may impact inhibition. An α, β-unsaturation carbonyl group and hydroxyl group in A-ring of cinnamic acid amide emerged to be critical functionalities for α-glucosidase inhibition. The molecular modeling study revealed that the inhibitory activities are tightly related to π-π interaction as well as hydrogen bond interaction between enzyme and inhibitors.
Anti-tyrosinase, antioxidant and antimicrobial activities of hydroxycinnamoylamides
Georgiev, Lyubomir,Chochkova, Maya,Totseva, Iskra,Seizova, Katya,Marinova, Emma,Ivanova, Galya,Ninova, Mariana,Najdenski, Hristo,Milkova, Tsenka
, p. 4173 - 4182 (2013/09/02)
Synthetic hydroxycinnamoylamides of amino acids (precursors of aromatic amines) were studied for their antioxidant activity in vitro by two antioxidant assay systems, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and inhibition of lipid peroxidation (LPO). Furthermore, these compounds were tested and compared with their corresponding cinnamoylamides of aromatic amines for their inhibitory activity using mushroom tyrosinase. In addition, five hydroxycinnamoyl amino acid amides were investigated for their antimicrobial effect. Structure-activity relationships analysis disclosed that the presence of catechol rest at amino acid or at benzene moieties of substituted cinnamic acid amides significantly scavenged DPPH radical and inhibited LPO. The results obtained by LPO clearly expressed the positive influence of indole moiety on the activity. Moreover, the existence of p-hydroxy substituted cinnamic acid moiety leads to better tyrosinase inhibition. Amongst the tested compounds, amides of p-coumaroyldopamine or tyramine and their corresponding amino acid precursors are the most potent tyrosinase inhibitors.
