884489-24-1Relevant academic research and scientific papers
Visible-Light-Promoted Decarboxylative Giese Reactions of α-Aryl Ethenylphosphonates and the Application in the Synthesis of Fosmidomycin Analogue
Guo, Ting,Zhang, Li,Fang, Yewen,Jin, Xiaoping,Li, Yan,Li, Ruifeng,Li, Xie,Cen, Wu,Liu, Xiaobo,Tian, Zongming
, p. 1352 - 1357 (2018/02/12)
An approach for the synthesis of α-aryl alkylphosphonates based on visible-light photocatalytic Giese reaction of α-aryl vinylphosphonates with aliphatic carboxylic acids has been successfully developed. This protocol tolerates a wide range of functional
DXR inhibition by potent mono- and disubstituted fosmidomycin analogues
Jansson, Anna M.,Wieì?ckowska, Anna,Bj?rkelid, Christofer,Yahiaoui, Samir,Sooriyaarachchi, Sanjeewani,Lindh, Martin,Bergfors, Terese,Dharavath, Shyamraj,Desroses, Matthieu,Suresh, Surisetti,Andaloussi, Mounir,Nikhil, Rautela,Sreevalli, Sharma,Srinivasa, Bachally R.,Larhed, Mats,Jones, T. Alwyn,Karlén, Anders,Mowbray, Sherry L.
, p. 6190 - 6199 (2013/09/02)
The antimalarial compound fosmidomycin targets DXR, the enzyme that catalyzes the first committed step in the MEP pathway, producing the essential isoprenoid precursors, isopentenyl diphosphate and dimethylallyl diphosphate. The MEP pathway is used by a number of pathogens, including Mycobacterium tuberculosis and apicomplexan parasites, and differs from the classical mevalonate pathway that is essential in humans. Using a structure-based approach, we designed a number of analogues of fosmidomycin, including a series that are substituted in both the Cα and the hydroxamate positions. The latter proved to be a stable framework for the design of inhibitors that extend from the polar and cramped (and so not easily druggable) substrate-binding site and can, for the first time, bridge the substrate and cofactor binding sites. A number of these compounds are more potent than fosmidomycin in terms of killing Plasmodium falciparum in an in vitro assay; the best has an IC50 of 40 nM.
Design, synthesis, and X-ray crystallographic studies of α-aryl substituted fosmidomycin analogues as inhibitors of mycobacterium tuberculosis 1-deoxy-d-xylulose 5-phosphate reductoisomerase
Andaloussi, Mounir,Henriksson, Lena M.,Wi?ckowska, Anna,Lindh, Martin,Bj?rkelid, Christofer,Larsson, Anna M.,Suresh, Surisetti,Iyer, Harini,Srinivasa, Bachally R.,Bergfors, Terese,Unge, Torsten,Mowbray, Sherry L.,Larhed, Mats,Jones, T. Alwyn,Karlén, Anders
, p. 4964 - 4976 (2011/10/01)
The natural antibiotic fosmidomycin acts via inhibition of 1-deoxy-d-xylulose 5-phosphate reductoisomerase (DXR), an essential enzyme in the non-mevalonate pathway of isoprenoid biosynthesis. Fosmidomycin is active on Mycobacterium tuberculosis DXR (MtDXR
ORGANOPHOSPHORIC DERIVATIVES USEFUL AS ANTI-PARASITIC AGENTS
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Page/Page column 33, (2008/06/13)
The present invention relates to novel phosphonic acid compounds having the structural formula (I): wherein: (a) R is a group of 1 to 5 substituents independently selected from the group consisting of fluoro, chloro, bromo, C1-4 alkoxy, C1
Synthesis of α-aryl-substituted and conformationally restricted fosmidomycin analogues as promising antimalarials
Haemers, Timothy,Wiesner, Jochen,Busson, Roger,Jomaa, Hassan,Van Calenbergh, Serge
, p. 3856 - 3863 (2007/10/03)
Fosmidomycin represents a new antimalarial drug that acts by inhibition of 1-deoxy-D-xylulose 5-phosphate reductoisomerase, an essential enzyme of the mevalonate-independent pathway of isoprenoid biosynthesis. This work describes the synthesis of a series
Synthesis of α-substituted fosmidomycin analogues as highly potent Plasmodium falciparum growth inhibitors
Haemers, Timothy,Wiesner, Jochen,Van Poecke, Sara,Goeman, Jan,Henschker, Dajana,Beck, Edwald,Jomaa, Hassan,Van Calenbergh, Serge
, p. 1888 - 1891 (2007/10/03)
In view of the promising antimalarial activity of fosmidomycin or its N-acetyl homologue FR900098, the objective of this work was to investigate the influence of aromatic substituents in the α-position of the phosphonate moiety. The envisaged analogues we
