1609349-56-5Relevant academic research and scientific papers
Divergent response of homologous ATP sites to stereospecific ligand fluorination for selectivity enhancement
Patel, Alpesh Ramanlal,Hardianto, Ari,Ranganathan, Shoba,Liu, Fei
, p. 1570 - 1574 (2017)
Acquiring a divergent response from homologous protein domains is essential for selective ligand-protein interactions. Stereospecific fluorination of (?)-balanol, an ATP mimic, uncovers a new source of selectivity from integrated chemical and conformational perturbation that differentiates homologous sites by the level of congruency in their response to local and remote fluorine effects.
Conformational regulation of substituted azepanes through mono-, di-, and trifluorination
Patel, Alpesh Ramanlal,Hunter, Luke,Bhadbhade, Mohan M.,Liu, Fei
, p. 2584 - 2593 (2014/05/06)
Substituted azepanes have flexible ring structures and this conformational diversity is important for their bioactivity. We have shown that a single fluorine atom, when installed diastereoselectively on a model azepane ring, can bias its ring to one major conformation. Here the conformational effects of mono-, di-, and trifluorination, as well as hydroxylation, on substituted azepanes have been investigated by 1H NMR spectroscopy and computational modeling in chloroform. Fluorine substitution was found to be more effective than hydroxyl group substitution in reducing conformational disorder; however, multiple fluorinations may not lead to additive conformational control and can result in complex conformational outcomes. Seven-membered nitrogen heterocycles have flexible ring structures and this conformational diversity is important for their bioactivity. Here the conformational effects of fluorination, as well as hydroxylation, on an azepane model system are investigated by 1H NMR spectroscopy and computational modeling. Copyright
