197588-25-3Relevant articles and documents
Rhodium(III)-Catalyzed Cascade Redox-Neutral C–H Functionalization and Aromatization: Synthesis of Unsymmetrical ortho-Biphenols
Hu, Zhiyong,Liu, Guixia
supporting information, p. 1643 - 1648 (2017/05/22)
An efficient rhodium(III)-catalyzed coupling reaction of N-aryloxyacetamides with 6-diazo-2-cyclohexenones through a cascade redox-neutral C–H functionalization and aromatization has been developed. This novel and scalable transformation provides a straightforward way to construct unsymmetrical ortho-biphenols with broad substrate scope under mild and redox-neutral conditions. The synthetic utility of this approach is demonstrated in the late-stage functionalization of bioactive compounds and the synthesis of an optically active ortho-biphenol. (Figure presented.).
Rhodium(III)-catalyzed C-H olefination for the Synthesis of ortho-alkenyl phenols using an oxidizing directing group
Shen, Yangyang,Liu, Guixia,Zhou, Zhi,Lu, Xiyan
, p. 3366 - 3369 (2013/07/26)
By using an oxidizing directing group, a mild, efficient Rh(III) catalyzed C-H olefination reaction between N-phenoxyacetamides and alkenes was developed. This reaction provided a straightforward way for the synthesis of ortho-alkenyl phenols, and the directing group is traceless in the product.
Fluorous tagged N-hydroxy phthalimide for the parallel synthesis of O-aryloxyamines
Gaucher-Wieczorek, Florence S.,Maillard, Ludovic T.,Badet, Bernard,Durand, Philippe
scheme or table, p. 655 - 658 (2010/10/21)
The parallel synthesis of O-aryloxyamines remains an unfulfilled need in the field of medicinal chemistry and fragment-based approaches. To fill this gap a solution-phase two-step process based on (1) a copper-catalyzed cross-coupling of aryl boronic acid
Bisaryloxime ethers as potent inhibitors of transthyretin amyloid fibril formation
Johnson, Steven M.,Petrassi, H. Michael,Palaninathan, Satheesh K.,Mohamedmohaideen, Nilofar N.,Purkey, Hans E.,Nichols, Christopher,Chiang, Kyle P.,Walkup, Traci,Sacchettini, James C.,Sharpless, K. Barry,Kelly, Jeffery W.
, p. 1576 - 1587 (2007/10/03)
Amyloid fibril formation by the plasma protein transthyretin (TTR), requiring rate-limiting tetramer dissociation and monomer misfolding, is implicated in several human diseases. Amyloidogenesis can be inhibited through native state stabilization, mediated by small molecule binding to TTR's primarily unoccupied thyroid hormone binding sites. New native state stabilizers have been discovered herein by the facile condensation of arylaldehydes with aryloxyamines affording a bisarylaldoxime ether library. Of the library's 95 compounds, 31 were active inhibitors of TTR amyloid formation in vitro. The bisaryloxime ethers selectively stabilize the native tetrameric state of TTR over the dissociative transition state under amyloidogenic conditions, leading to an increase in the dissociation activation barrier. Several bisaryloxime ethers bind selectively to TTR in human blood plasma over the plethora of other plasma proteins, a necessary attribute for efficacy in vivo. While bisarylaldoxime ethers are susceptible to degradation by N-O bond cleavage, this process is slowed by their binding to TTR. Furthermore, the degradation rate of many of the bisarylaldoxime ethers is slow relative to the half-life of plasma TTR. The bisaryloxime ether library provides valuable structure-activity relationship insight for the development of structurally analogous inhibitors with superior stability profiles, should that prove necessary.
