6214-45-5Relevant articles and documents
Structure-activity relationship (SAR) studies on the mutagenic properties of 2,7-diaminofluorene and 2,7-diaminocarbazole derivatives
Kim, Byeong Wook,Lee, Hwa,Keum, Gyochang,Kim, B. Moon
supporting information, (2020/11/27)
We discovered that 2,7-diaminofluorene or 2,7-diaminocarbazole moiety can be employed as a core structure of highly effective NS5A inhibitors that are connected through amide bonds to proline-valine-carbamate motifs. Amide bonds can be easily cleaved via various metabolic pathways upon administration into the body, and metabolites containing 2,7-diaminofluorene and 2,7-diaminocarbazole core structures have been known to be strong mutagens. To avoid the mutagenesis issue of these core structures, we examined various functional groups at the C9 or N9 position of 2,7-diaminofluorene or 2,7-diaminocarbazole, respectively, through the Ames test in TA98 and TA100 mutants of Salmonella typhimurium LT-2. We discovered that, through proper alkyl substitution at the C9 or N9 position, 2,7-diaminofluorene and 2,7-diaminocarbazole moieties can be successfully employed in drug discovery without necessarily causing mutagenicity problems.
New convergent one pot synthesis of amino benzyl ethers bearing a nitrogen-containing bicycle
López, Jhon J.,Pérez, Edwin G.
, p. 715 - 723 (2019/02/19)
We report herein a new convergent one pot method for the synthesis of amino benzyl ethers containing a bicyclic amine, derived from different substituted benzyl alcohols and bicyclic amino alcohols such as tropine, pseudotropine, and 3-quinuclidinol, using chlorotrimethylsilane and sodium iodide. In order to avoid the competitive reaction with the nitrogen atom, a solution of the separately prepared alkoxide of tropine, pseudotropine, and 3-quinuclidinol was added to the preformed substituted benzyl iodides and allowed to reflux at 90 °C for 15 h under nitrogen atmosphere. This method provides an efficient alternative of the preparation of amino benzyl ethers in organic synthesis with good yields in comparison with existed methods.
Chemoselective and site-selective peptide and native protein modification enabled by aldehyde auto-oxidation
Purushottam, Landa,Adusumalli, Srinivasa Rao,Chilamari, Maheshwerreddy,Rai, Vishal
supporting information, p. 959 - 962 (2017/01/17)
We report a chemoselective and site-selective formylation of ?-amine in native proteins. The aldehyde auto-oxidation re-routing, regulated generation of formate, and reversible N-terminus protection drive the transformation. It labels a single ?-amine in a pool of its copies, other nucleophilic residues, and α-amine. The extension of the methodology leads to site-selective acylation.
