20215-79-6Relevant academic research and scientific papers
Cavity-containing supramolecular gels as a crystallization tool for hydrophobic pharmaceuticals
Kaufmann, Lena,Kennedy, Stuart R.,Jones, Christopher D.,Steed, Jonathan W.
, p. 10113 - 10116 (2016)
We present two approaches to low-molecular-weight supramolecular gels bearing hydrophobic cavities based on calixarene-containing building blocks. Gels are formed by a calixarene based tetrahydrazide gelator or a co-gel of a calixarene diammonium salt and
Dual-action inhibitors of HIF prolyl hydroxylases that induce binding of a second iron ion
Yeoh, Kar Kheng,Chan, Mun Chiang,Thalhammer, Armin,Demetriades, Marina,Chowdhury, Rasheduzzaman,Tian, Ya-Min,Stolze, Ineke,McNeill, Luke A.,Lee, Myung Kyu,Woon, Esther C. Y.,MacKeen, Mukram M.,Kawamura, Akane,Ratcliffe, Peter J.,Mecinovi?, Jasmin,Schofield, Christopher J.
supporting information, p. 732 - 745 (2013/02/26)
Inhibition of the hypoxia-inducible factor (HIF) prolyl hydroxylases (PHD or EGLN enzymes) is of interest for the treatment of anemia and ischemia-related diseases. Most PHD inhibitors work by binding to the single ferrous ion and competing with 2-oxoglutarate (2OG) co-substrate for binding at the PHD active site. Non-specific iron chelators also inhibit the PHDs, both in vitro and in cells. We report the identification of dual action PHD inhibitors, which bind to the active site iron and also induce the binding of a second iron ion at the active site. Following analysis of small-molecule iron complexes and application of non-denaturing protein mass spectrometry to assess PHD2·iron· inhibitor stoichiometry, selected diacylhydrazines were identified as PHD2 inhibitors that induce the binding of a second iron ion. Some compounds were shown to inhibit the HIF hydroxylases in human hepatoma and renal carcinoma cell lines. The Royal Society of Chemistry 2013.
