879216-11-2Relevant academic research and scientific papers
Anti-Markovnikov Hydroazidation of Alkenes by Visible-Light Photoredox Catalysis
Wang, Juan-Juan,Yu, Wei
supporting information, p. 3510 - 3514 (2019/02/19)
The anti-Markovnikov hydroazidation of alkenes has been accomplished under visible-light irradiation by using [Ir(dF(CF3)ppy)2(dtbbpy)]PF6 as the photocatalyst and trimethylsilyl azide as the azidating agent. The reactions were greatly facilitated by water, the beneficial effect of which can be attributed to its participation in the reaction as the hydrogen donor, as indicated by deuterium isotope experiments. The reactions proceed under solvent free conditions in the presence of water. 4-Dimethylaminopyridine also exhibited a beneficial effect on the reactions. The present method enabled hydroazidation of several types of unactivated alkenes with good yields and high regioselectivity.
New synthetic routes for N-substituted 1,n-diamines. II. Synthesis of selectively N-substituted tetra- and pentamethylenediamines from ω-alkanoic acid derivatives
Ramírez, María A.,Corona, María V.,Ortiz, Gisela,Salerno, Alejandra,Perillo, Isabel A.,Blanco, María M.
, p. 1466 - 1468 (2011/06/10)
A new approach for the synthesis of selectively N-substituted tetra- and pentamethylenediamines 1 (n = 4,5) is described. The method uses N-substituted ω-haloalkanamides 2 as precursors and involves the microwave-promoted conversion into ω-azidocarboxamides 3 and later the reduction of both azido and carboxamide groups with diborane.
Rapid assembly and in situ screening of bidentate inhibitors of protein tyrosine phosphatases
Srinivasan, Rajavel,Uttamchandani, Mahesh,Yao, Shao Q.
, p. 713 - 716 (2007/10/03)
We have successfully designed and synthesized a small library of protein tyrosine phosphatase (PTP) inhibitors, in which the so-called "click chemistry" or Cu(I)-catalyzed 1,3-dipolar alkyne-azide coupling reaction was carried out for rapid assembly of 66 different bidentate compounds. Subsequent in situ enzymatic screening revealed a potential PTP1B inhibitor (IC50 = 4.7 μM) which is 10-100 fold more potent than other PTPs.
