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See detailN1-Fluoroalkyltryptophan analogues: synthesis and in vitro study as potential substrates for indoleamine 2,3-dioxygenase
Henrottin, Jean ULg; Zervosen, Astrid ULg; Lemaire, Christian ULg et al

in ACS Medicinal Chemistry Letters (2015)

ABSTRACT: Indoleamine 2,3-dioxygenase (hIDO) is an enzyme that catalyzes the oxidative cleavage of the indole ring of L-tryptophan through the kynurenine pathway, thereby exerting immunosuppressive ... [more ▼]

ABSTRACT: Indoleamine 2,3-dioxygenase (hIDO) is an enzyme that catalyzes the oxidative cleavage of the indole ring of L-tryptophan through the kynurenine pathway, thereby exerting immunosuppressive properties in inflammatory and tumoral tissues. The syntheses of 1-(2-fluoroethyl)-tryptophan (1-FETrp) and 1-((1-(2-fluoroethyl)-1H-1,2,3-triazol-4-yl)methyl)-tryptophan, two N1-fluoroalkylated tryptophan derivatives, are described here. In vitro enzymatic assays with these two new potential substrates of hIDO show that 1-FETrp is a good and specific substrate of hIDO. Therefore, its radioactive isotopomer, 1-[18F]FETrp, should be a molecule of choice to visualize tumoral and inflammatory tissues and/or to validate new potential inhibitors. [less ▲]

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See detailEnhancing a CH-pi interaction to increase the affinity for 5-HT1A receptors
Liégeois, Jean-François ULg; Lespagnard, Marc; Meneses Salas, Elsa et al

in ACS Medicinal Chemistry Letters (2014), 5

An electrostatic interaction related to a favourable position of the distal phenyl ring and a phenylalanine residue in the binding pocket would explain the higher 5-HT1A affinity of a 4-phenyl-1,2,3,6 ... [more ▼]

An electrostatic interaction related to a favourable position of the distal phenyl ring and a phenylalanine residue in the binding pocket would explain the higher 5-HT1A affinity of a 4-phenyl-1,2,3,6-tetrahydropyridine (THP) analogue compared to the corresponding 4-phenylpiperazine analogue. To explore a possible reinforcement of this interaction to increase the affinity for 5-HT1A receptors, different 4-substituted-phenyl analogues were synthesized and tested. The most important increase of affinity is obtained with two electron-donating methyl groups in position 3 and 5 [less ▲]

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See detailStructure Guided Development of Potent Reversibly Binding Penicillin Binding Protein Inhibitors
Woon, Esther C. Y.; Zervosen, Astrid ULg; Sauvage, Eric ULg et al

in ACS Medicinal Chemistry letters (2011), 2 (3)

Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein ... [more ▼]

Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as β-lactams. [less ▲]

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See detailNH-1,2,3-Triazole-based Inhibitors of the VIM-2 Metallo-β- Lactamase: Synthesis and Structure-Activity Studies
Weide, Timo; Saldanha, S. Adrian; Minond, Dmitriy et al

in ACS Medicinal Chemistry Letters (2010), 1(4)

Metallo-ß-lactamases (MBL) are an emerging cause of bacterial resistance to antibiotic treatment. The VIM-2 ß-lactamase is the most commonly encountered MBL in clinical isolates worldwide. Described here ... [more ▼]

Metallo-ß-lactamases (MBL) are an emerging cause of bacterial resistance to antibiotic treatment. The VIM-2 ß-lactamase is the most commonly encountered MBL in clinical isolates worldwide. Described here are potent and selective small molecule inhibitors of VIM-2 containing the arylsulfonyl-NH-1,2,3-triazole chemotype that potentiate the efficacy of the ß-lactam, imipenem, in E. coli. [less ▲]

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