Jacques Renault
University of Rennes
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Featured researches published by Jacques Renault.
Bioorganic & Medicinal Chemistry Letters | 1998
Sophie Tomasi; Myriam Le Roch; Jacques Renault; Jean-Charles Corbel; Philippe Uriac; Bertrand Carboni; Damien Moncoq; Bénédicte Martin; Jean-Guy Delcros
A series of N1-monosubstituted putrescine and spermine derivatives was synthesised using a solid phase methodology. We evaluated their cytotoxicity, calmodulin antagonism and polyamine uptake inhibition, pharmacological properties shared by some antitumoral agents.
Journal of Organic Chemistry | 2013
Khanh Hung Nguyen; Sophie Tomasi; Myriam Le Roch; Loïc Toupet; Jacques Renault; Philippe Uriac; Nicolas Gouault
A rapid and efficient one-step halopyridone synthesis has been developed based on gold-catalyzed cyclization of β-amino-ynone intermediates and halodeauration process.
Journal of Medicinal Chemistry | 2010
Sophie Tomasi; Jacques Renault; Bénédicte Martin; Stéphane Duhieu; Virginie Cerec; Myriam Le Roch; Philippe Uriac; Jean-Guy Delcros
The polyamine transport system (PTS) whose activity is up-regulated in cancer cells is an attractive target for drug design. Two heterocyclic (azepine and benzazepine) systems were conjugated to various polyamine moieties through an amidine bound to afford 18 compounds which were evaluated for their affinity for the PTS and their ability to use the PTS for cell delivery. Structure-activity relationship studies and lead optimization afforded two attractive PTS targeting compounds. The azepine-spermidine conjugate 14 is a very selective substrate of the PTS that may serve as a vector for radioelements used for diagnoses or therapeutics in nuclear medicine. The nitrobenzazepine-spermine conjugate 28 is a very powerful PTS inhibitor with very low intrinsic cytotoxicity, able to prevent the growth of polyamine depleted cells in presence of exogenous polyamines.
Tetrahedron Letters | 2001
Jacques Renault; Marina Lebranchu; Anne Lecat; Philippe Uriac
Abstract A systematic study of nucleophilic displacement of mesyl groups using benzylamine was carried out on Multipin Synphase™ supports. The optimal conditions were applied for the combinatorial synthesis of polyamine derivatives from commercially available aminoalcohols and amines.
The International Journal of Biochemistry & Cell Biology | 2000
Nikolaus Seiler; Benoı̂t Duranton; F Vincent; Francine Gossé; Jacques Renault; Francis Raul
N(1)-(n-octanesulfonyl)spermine (N(1) OSSpm) is a substrate of polyamine oxidase. It shares several properties with spermine, such as antagonism of NMDA-type glutamate receptors, calmodulin antagonism, and cytotoxicity, but it is more potent by orders of magnitude in these regards than spermine. The human colon carcinoma-derived cell line CaCo-2 was used as a model to study the toxicity of N(1) OSSpm as a function of polyamine oxidase (PAO) activity and differentiation. If the formation of hydrogen peroxide and aminoaldehyde by the PAO-catalysed reactions was prevented by selective inactivation of the enzyme with MDL 72527, cytotoxicity of N(1)OSSpm was not diminished, but on the contrary, enhanced. Exponentially growing CaCo-2 cells were considerably more sensitive to N(1)OSSpm than differentiating cells. The results suggest that cytotoxic substrates of PAO exhibit enhanced cytotoxicity in cells, if PAO activity is inhibited. Since tumour cells are known to have lower polyamine oxidase activities than their normal counterparts, it will be interesting to explore whether cytotoxic substrates of polyamine oxidase, for which N(1)OSSpm is an example, are suited to preferentially kill tumour cells.
Nucleosides, Nucleotides & Nucleic Acids | 1994
Jacques Renault; Daniel Laduree; Max Robba
Abstract Acyclic nucleosides were prepared by alkylation of dihydrothieno and thianopyrimidines diones following Vorbruggen and Niedballas method.(1) None of these HEPT analogues showed significant activity against Human Immunodeficiency Virus-1 (HIV-1)
Brain Research | 2004
Brian Kirby; Sheila A. Ryder; Nikolaus Seiler; Jacques Renault; Graham G. Shaw
The potential polyamine antagonist action of N1-dansyl-spermine (a potent NMDA antagonist) was assessed in two in vivo mouse models of polyamine action. Co-administration of N1-dansyl-spermine (2-10 microg, i.c.v.) with spermine (100 microg, i.c.v.) resulted in a dose-dependent antagonism of the spermine-induced CNS excitation (body tremor and fatal tonic convulsions). In addition, the same dose of N1-dansyl-spermine antagonised spermines enhancement of NMDA-induced convulsions. These results suggest that N1-dansyl-spermine is in vivo a potent antagonist of the CNS effects of spermine and of its action at the positive polyamine modulatory site on the NMDA receptor.
Bioorganic & Medicinal Chemistry Letters | 2010
Mickaël Jean; Jacques Renault; Nicolas Levoin; Denis Danvy; Thierry Calmels; Isabelle Berrebi-Bertrand; Philippe Robert; Jean Schwartz; Jeanne-Marie Lecomte; Philippe Uriac; Marc Capet
Isosteric replacement of the amide function and modulation of the arylpiperazine moiety of known dopamine D3 receptor ligands led to potent and selective compounds. Enhanced bioavailability and preferential brain distribution make compound 6c a good candidate for pharmacological and clinical evaluation.
Molecular Immunology | 1999
Nathalie Bouillé; Julie Johnston; Anne Royou; Isabelle Debroise; Myriam Le Roch; Jacques Renault; Jacques-Philippe Moulinoux; Jean-Guy Delcros
The structural basis of the binding of the polyamine spermine to the monoclonal antibody SPM8-2 was studied using computer modelling, ELISA methods and chemical modifications of the binding site residues. Paratope modelling showed that the antibody combining site forms a highly negatively charged cavity mainly shaped by aspartic acid and tyrosine residues which contact the tetra-positively charged spermine molecule by electrostatic interactions and hydrogen bondings. The importance of the electrostatic environment for spermine binding to SPM8-2 is emphasised by the strong dependency on pH and ionic strength. Specific chemical modifications of carboxylate groups and tyrosine residues of the antibody adsorbed to microtiter plates resulted in decreased binding of the N1-biotin-spermine conjugate used to monitor the activity of the antibody. These observations are consistent with a key role of aspartate and tyrosine residues in complex formation with spermine. These studies, important to our understanding of antibody-hapten specificity, may also shed light on important motifs responsible for protein-polyamine interactions.
Tetrahedron Letters | 2003
Myriam Le Roch; Jacques Renault; Kristell Penlaë; Philippe Uriac
The opening of protected erythronolactone by an amine or a diamine furnished hydroxy-amides. Their multistep functional conversion led to either selectively protected or free dihydroxy-polyamines.