173458-34-9Relevant academic research and scientific papers
Visible light sensitization of benzoyl azides: Cascade cyclization toward oxindoles: Via a non-nitrene pathway
Bagal, Dattatraya B.,Park, Sung-Woo,Song, Hyun-Ji,Chang, Sukbok
supporting information, p. 8798 - 8801 (2017/08/09)
Visible light sensitization of benzoyl azides was examined in reaction with N-phenylmethacrylamides to afford biologically important oxindoles and spirooxindoles via a cascade cyclization under mild reaction conditions. Mechanistic studies suggested a non-nitrene pathway, where triplet benzoyl azides act as the reactive intermediate.
Orthogonal reactivity of acyl azides in C-H activation: Dichotomy between C-C and C-N amidations based on catalyst systems
Shin, Kwangmin,Ryu, Jaeyune,Chang, Sukbok
supporting information, p. 2022 - 2025 (2014/05/06)
The dual reactivity of acyl azides was utilized successfully in C-H activation by the choice of catalyst systems: while selective C-C amidation was achieved under thermal Rh catalysis, a Ru catalyst was found to mediate direct C-N amidation also highly se
Oxidative amidation and azidation of aldehydes by NHC catalysis
De Sarkar, Suman,Studer, Armido
supporting information; experimental part, p. 1992 - 1995 (2010/07/10)
Figure presented N-Heterocyclic carbene catalyzed oxidative amidations of various aldehydes to the corresponding hexafluoroisopropylesters by using the readily available organic oxidant A are described. The hexafluoroisopropylesters prepared in situ are shown to be highly useful active esters for amide bond formation. In addition, oxidative azidation of aldehydes is presented. These mild organocatalytic processes do not use any transition metal.
Tyrosine kinase inhibitors. 4. Structure-activity relationships among N- and 3-substituted 2,2'-dithiobis(1H-indoles) for in vitro inhibition of receptor and nonreceptor protein tyrosine kinases
Palmer,Rewcastle,Thompson,Boyd,Showalter,Sercel,Fry,Kraker,Denny
, p. 58 - 67 (2007/10/02)
A series of 3-substituted 2,2'-dithiobis(1H-indoles) were synthesized and evaluated for their ability to inhibit the tyrosine kinase activity of both the epidermal growth factor receptor (EGFR) and the nonreceptor pp60(v-src) tyrosine kinase, to extend the available structure-activity relationships for this series. The majority of the compounds were prepared either by reaction of 2-chloro-1-methylindole-3-carbonyl chloride with amines, followed by thiomethylation, demethylation, and oxidative dimerization, or by reaction of isocyanates with the anion of 1-methyl-2-indolinethione followed by dimerization. Overall, inhibitory activity is retained by analogues having a wide variety of side chains. A series of 3-carboxamide analogues had moderate to good activity against isolated EGFR (IC50s 1-20 μM), with monoalkyl substitution of the carboxamide being optimal. Polar side chains were generally less effective than lipophilic ones, with benzyl being particularly effective. However, N,N-disubstitution was the most effective pattern for inhibition of pp60(v-src). A variety of substituted N-phenylcarboxamides had lower activity against EGFR than the parent derivative, and a N- thienylcarboxamide also had low activity. A series of 3-ketones, including methyl, phenyl, and furyl derivatives, showed moderate activity against the pp60(v-src) kinase, but were less effective against EGFR. The mechanism of inhibition of both kinases by these drugs was shown to be noncompetitive with respect to both ATP and peptide substrate. Selected compounds inhibited the growth of Swiss 3T3 cells with IC50s in the low micromolar range and inhibited bFGF-mediated intracellular tyrosine phosphorylation in the same cell line. Thiol inhibits the effects of the compounds, suggesting that one possible mechanism of inhibition is thiol-disulfide exchange with thiol- containing residues in the catalytic sites. Crystal structures of two representative compounds show a folded, V-shaped structure, with the disulfide bridge exposed, consistent with this hypothesis.
