149603-85-0Relevant academic research and scientific papers
Structure activity relationship studies on rhodanines and derived enethiol inhibitors of metallo-β-lactamases
Zhang, Dong,Markoulides, Marios S.,Stepanovs, Dmitrijs,Rydzik, Anna M.,El-Hussein, Ahmed,Bon, Corentin,Kamps, Jos J.A.G.,Umland, Klaus-Daniel,Collins, Patrick M.,Cahill, Samuel T.,Wang, David Y.,von Delft, Frank,Brem, Jürgen,McDonough, Michael A.,Schofield, Christopher J.
supporting information, p. 2928 - 2936 (2018/04/19)
Metallo-β-lactamases (MBLs) enable bacterial resistance to almost all classes of β-lactam antibiotics. We report studies on enethiol containing MBL inhibitors, which were prepared by rhodanine hydrolysis. The enethiols inhibit MBLs from different subclasses. Crystallographic analyses reveal that the enethiol sulphur displaces the di-Zn(II) ion bridging ‘hydrolytic’ water. In some, but not all, cases biophysical analyses provide evidence that rhodanine/enethiol inhibition involves formation of a ternary MBL enethiol rhodanine complex. The results demonstrate how low molecular weight active site Zn(II) chelating compounds can inhibit a range of clinically relevant MBLs and provide additional evidence for the potential of rhodanines to be hydrolysed to potent inhibitors of MBL protein fold and, maybe, other metallo-enzymes, perhaps contributing to the complex biological effects of rhodanines. The results imply that any medicinal chemistry studies employing rhodanines (and related scaffolds) as inhibitors should as a matter of course include testing of their hydrolysis products.
Catalytic enantioselective synthesis of tertiary thiols from 5h-thiazol-4-ones and nitroolefins: Bifunctional ureidopeptide-based bronsted base catalysis
Diosdado, Saioa,Etxabe, Julen,Izquierdo, Joseba,Landa, Aitor,Mielgo, Antonia,Olaizola, Iurre,Lopez, Rosa,Palomo, Claudio
supporting information, p. 11846 - 11851 (2013/11/19)
Fully loaded: The ureidopeptide-based bifunctional Bronsted base 1 efficiently promotes the first direct catalytic Michael reaction of α-mercapto carboxylate surrogates with nitroolefins involving a fully substituted α-carbon atom construction. Copyright
Process for the synthesis of α-substituted acrylic acids and their application
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, (2008/06/13)
Process for the synthesis of a-substituted acrylic acids and their application. Process for the synthesis of a-substituted acrylic acids of general formula (I) and their application to the synthesis of N- (mercaptoacyl) aminoacid derivatives of formula (II). STR1
Mercaptoacyl matrix metalloproteinase inhibitors: The effect of substitution at the mercaptoacyl moiety
Baxter, Andrew D.,Bhogal, Ranjev,Bird, John B.,Buckley, George M.,Gregory, David S.,Hedger, Paul C.,Manallack, David T.,Massil, Tracy,Minton, Kevin J.,Montana, John G.,Neidle, Stephen,Owen, David A.,Watson, Robert J.
, p. 2765 - 2770 (2007/10/03)
The in vitro potency of orally-active mercaptoacyl matrix metalloproteinase inhibitors is increased by the introduction of appropriate substitutents on the mercaptoacyl moiety.
