- Silver-Mediated Trifluoromethoxylation of (Hetero)aryldiazonium Tetrafluoroborates
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Here we report a silver-mediated trifluoromethoxylation of (hetero)aryldiazonium tetrafluoroborates by converting an aromatic amino group into an OCF3 group. This method, which can be considered to be a trifluoromethoxylation variation of the classic Sandmeyer-type reaction, uses readily available aryl and heteroaromatic amines as starting materials and AgOCF3 as trifluoromethoxylating reagents. The broad substrate scope and simple, mild reaction condition made this transformation a valuable method in constructing aryl-OCF3 bonds.
- Yang, Yu-Ming,Yao, Jian-Fei,Yan, Wei,Luo, Zhuangzhu,Tang, Zhen-Yu
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supporting information
p. 8003 - 8007
(2019/10/11)
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- NEW AMIDINO DERIVATIVES AND THEIR USE AS THROMBIN INHIBITORS
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There is provided compounds of formula Iwherein R, Rx, Y, R, n and B have meanings given in the description which are useful as competitive inhibitors of trypsin-like proteases, such as thrombin, and in particular in the treatment of conditions wher
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- N-HYDROXYAMIDE DERIVATIVES POSSESSING ANTIBACTERIAL ACTIVITY
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Novel N-hydroxyamide derivatives are disclosed. These N-hydroxyamide derivatives inhibit UPD-3O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase, an enzyme present in gram negative bacteria and are therefore useful as antimicrobials and antibiotics. Methods of synthesis and of use of the compounds are also disclosed.
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- Potent, novel in vitro inhibitors of the Pseudomonas aeruginosa deacetylase LpxC
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Deacetylation of uridyldiphospho-3-O-(R-hydroxydecanoyl)-N-acetylglucosamine by LpxC is the first committed step in the Pseudomonas aeruginosa biosynthetic pathway to lipid A; homologous enzymes are found widely among Gram-negative bacteria. As an essential enzyme for which no inhibitors have yet been reported, the P. aeruginosa LpxC represents a highly attractive target for a novel antibacterial drug. We synthesized several focused small-molecule libraries, each composed of a variable aromatic ring, one of four heterocyclic/spacer moieties, and a hydroxamic acid and evaluated the LpxC inhibition of these compounds against purified P. aeruginosa enzyme. To ensure that the in vitro assay would be as physiologically relevant as possible, we synthesized a tritiated form of the specific P. aeruginosa glycolipid substrate and measured directly the enzymatically released acetate. Several of our novel compounds, predominantly those having fluorinated substituents on the aromatic ring and an oxazoline as the heterocyclic moiety, demonstrated in vitro IC50 values less than 1 μM. We now report the synthesis and in vitro evaluation of these P. aeruginosa LpxC inhibitors.
- Kline, Toni,Andersen, Niels H.,Harwood, Eric A.,Bowman, Jason,Malanda, Andre,Endsley, Stephanie,Erwin, Alice L.,Doyle, Michael,Fong, Susan,Harris, Alex L.,Mendelsohn, Brian,Mdluli, Khisimuzi,Raetz, Christian R. H.,Stover, C. Kendall,Witte, Pamela R.,Yabannavar, Asha,Zhu, Shuguang
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p. 3112 - 3129
(2007/10/03)
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