128184-26-9Relevant academic research and scientific papers
Cross-Coupling of Primary Amides to Aryl and Heteroaryl Partners Using (DiMeIHeptCl)Pd Promoted by Trialkylboranes or B(C6F5)3
Sharif, Sepideh,Day, Jonathan,Hunter, Howard N.,Lu, Yu,Mitchell, David,Rodriguez, Michael J.,Organ, Michael G.
supporting information, p. 18436 - 18439 (2018/01/08)
Boron-derived Lewis acids have been shown to effectively promote the coupling of amide nucleophiles to a wide variety of oxidative addition partners using Pd-NHC catalysts. Through a combination of NMR spectroscopy and control studies with and without oxygen and radical scavengers, we propose that boron-imidates form under the basic reaction conditions that aid coordination of nitrogen to Pd(II), which is rate limiting, and directly delivers the intermediate for reductive elimination.
Structure-based modification of 3-/4-aminoacetophenones giving a profound change of activity on tyrosinase: From potent activators to highly efficient inhibitors
You, Ao,Zhou, Jie,Song, Senchuan,Zhu, Guoxun,Song, Huacan,Yi, Wei
, p. 255 - 262 (2015/03/04)
In this study, we developed 3-/4-aminoacetophenones and their structure-based 3-/4-aminophenylethylidenethiosemicarbazide derivatives, respectively, as novel tyrosinase activators and inhibitors. Notably, all the obtained thiosemicarbazones displayed more potent tyrosinase inhibitory activities than kojic acid. Especially, compound 7k was found to be the most active tyrosinase inhibitor with IC50 value of 0.291 1/4M. The structure-activity relationships (SARs) analysis showed that: (1) the amine group was absolutely necessarily for determining the tyrosinase activation activity; (2) the introduction of thiosemicarbazide group played a very vital role in transforming tyrosinase activators into tyrosinase inhibitors; (3) the phenylethylenethiosemicarbazide moiety was crucial for determining the tyrosinase inhibitory activity; (4) the type of acyl group had no obvious effect on the inhibitory activity; (5) the position of amide substituent on the phenyl ring influenced the tyrosinase inhibitory potency. Moreover, the inhibition mechanism and inhibition kinetics study revealed that compound 7k was reversible and non-competitive inhibitor, and compound 8h was reversible and competitive-uncompetitive mixed-II type inhibitor.
Nickel-catalyzed dehydrogenative cross-coupling: Direct transformation of aldehydes into esters and amides
Whittaker, Aaron M.,Dong, Vy M.
supporting information, p. 1312 - 1315 (2015/01/30)
By exploring a new mode of nickel-catalyzed cross-coupling, a method to directly transform both aromatic and aliphatic aldehydes into either esters or amides has been developed. The success of this oxidative coupling depends on the appropriate choice of catalyst and organic oxidant, including the use of either α,α,α-trifluoroacetophenone or excess aldehyde. Mechanistic data that supports a catalytic cycle involving oxidative addition into the aldehyde C-H bond is also presented.
Synthesis and biological activity of strongly fluorescent tricyclic analogues of acyclovir and ganciclovir
Goslinski, Tomasz,Golankiewicz, Bozenna,De Clercq, Erik,Balzarini, Jan
, p. 5052 - 5057 (2007/10/03)
In search of strongly fluorescent tricyclic analogues of acyclovir (ACV, 1) and ganciclovir (GCV, 2), derivatives of the 3,9-dihydro-9-oxo-5H-imidazo[1,2-α]purine system, several 6-[4- (acyloxy)-phenyl], 6-[4-(acylamino)phenyl], and 6-[4-(phenoxycarbonyloxy)phenyl]-substituted TACV and TGCV analogues were synthesized and evaluated for their activity against herpes simplex virus types 1 and 2 in cell culture. All TACV and TGCV analogues showed strong fluorescence (quantum yield of 30-65% vs 2-aminopurine 100%). The 6-[4-(phenoxycarbonyloxy)phenyl]-substituted compounds 11 and 19 displayed the best combination of the fluorescence and antiviral potency.
A light-activated antibody catalyst
Taylor, Matthew J.,Hoffman, Timothy Z.,Yli-Kauhaluoma, Jari T.,Lerner, Richard A.,Janda, Kim D.
, p. 12783 - 12790 (2007/10/03)
A catalytic antibody for a multistep Norrish type II photochemical reaction was investigated. Absorption of light energy by α-ketoamide substrate 1b produced a high-energy biradical intermediate, that was then directed by the antibody microenvironment to form tetrahydropyrazine 13 with a k(cat) of 1.4 x 10-3 min-1 at 280 nm irradiation and an enantiomeric excess of 78%. Antibody-catalyzed reactions performed with radiolabeled substrate indicated that little self-inactivation (6.8 mol % covalent modification after four turnovers per antibody) occurred. The singular product obtained in the antibody-catalyzed reaction was not observed in the uncatalyzed reaction unless the pH was lowered below 4. Studies suggested that the interplay of conformational control and chemical catalysis were responsible for the high specificity. A change in protonation state of the antibody was correlated with the inclusion of a new reaction pathway in the antibody-catalyzed reaction, indicating that general-base catalysis was involved in the rerouting of the Norrish reaction to form 13. An X-ray crystal structure of the substrate was obtained and suggested that the antibody binds the α-ketoamide in a twisted conformation optimal for the first step of the photochemical reaction. The antibody described here is a model for the evolution of light-activated enzymes and can serve as a foundation for the development of light-dependent antibody catalysts for a range of even more complex photochemical reactions.
