Arnaud Bondon
University of Rennes
Network
Latest external collaboration on country level. Dive into details by clicking on the dots.
Publication
Featured researches published by Arnaud Bondon.
Tetrahedron | 2002
Jacques Leroy; Emmanuel Porhiel; Arnaud Bondon
Abstract The synthesis of partially β-fluorinated meso -tetraphenylporphyrins using Lindsey conditions, has been examined, starting either from 3,4-difluoro-1 H -pyrrole or from 3-fluoro-1 H -pyrrole. In the case of the first synthon, condensation with pyrrole and benzaldehyde afforded a mixture of porphyrins of general formula β-F n TPP ( n =0,2,4,6,8) displaying linearly correlated spectroscopic and electrochemical properties. With the second synthon, condensation with benzaldehyde produced an unresolvable mixture of β-tetrafluoroporphyrins presenting spectroscopic and electrochemical properties in coherence with those observed in the first case. Preliminarily, the synthesis and isolation of the hitherto unknown 3-fluoro-1 H -pyrrole has been approached via several methods.
Journal of Medicinal Chemistry | 2010
Frédérik Oger; Aurélien Lecorgne; Elisa Sala; Vanessa Nardese; Florence Demay; Soizic Chevance; Danielle C. Desravines; Nataliia Aleksandrova; Rémy Le Guével; Simone Lorenzi; Andrea R. Beccari; Peter Barath; Darren J. Hart; Arnaud Bondon; Daniele Carettoni; Gérard Simonneaux; Gilles Salbert
Inhibition of histone deacetylases (HDACs) leads to growth arrest, differentiation, or apoptosis of tumor cell lines, suggesting HDACs as promising targets for cancer therapy. At present, only one HDAC inhibitor (HDACi) is used in therapy: suberoylanilide hydroxamic acid (SAHA). Here, we describe the synthesis and biological evaluation of a new series of compounds derived from SAHA by substituting short alkyl chains at various positions of the phenyl ring. Such modifications induced variable effects ranging from partial loss of activity to increased potency. Through molecular modeling, we describe a possible interaction between HDAC7 proline 809, a residue that is strictly conserved within class 2 enzymes only, and the amide group of HDACi, while nuclear magnetic resonance experiments indicated that dimethyl m-substitution may stabilize the inhibitor in the active site. Our data provide novel information on the structure-activity relationship of HDACi and suggest new ways for developing second generation SAHA-like molecules.
Journal of Biological Chemistry | 2009
Sébastien Legardinier; Baptiste Legrand; Céline Raguénès-Nicol; Arnaud Bondon; Serge Hardy; Christophe Tascon; Elisabeth Le Rumeur; Jean-François Hubert
Lack of functional dystrophin causes severe Duchenne muscular dystrophy. The subsarcolemmal location of dystrophin, as well as its association with both cytoskeleton and membrane, suggests a role in the mechanical regulation of muscular membrane stress. In particular, phenotype rescue in a Duchenne muscular dystrophy mice model has shown that some parts of the central rod domain of dystrophin, constituted by 24 spectrin-like repeats, are essential. In this study, we made use of rare missense pathogenic mutations in the dystrophin gene and analyzed the biochemical properties of the isolated repeat 23 bearing single or double mutations E2910V and N2912D found in muscle dystrophy with severity grading. No dramatic effect on secondary and tertiary structure of the repeat was found in mutants compared with wild type as revealed by circular dichroism and NMR. Thermal and chemical unfolding data from circular dichroism and tryptophan fluorescence show significant decrease of stability for the mutants, and stopped-flow spectroscopy shows decreased refolding rates. The most deleterious single mutation is the N2912D replacement, although we observe additive effects of the two mutations on repeat stability. Based on three-dimensional structures built by homology molecular modeling, we discuss the modifications of the mutation-induced repeat stability. We conclude that the main forces involved in repeat stability are electrostatic inter-helix interactions that are disrupted following mutations. This study represents the first analysis at the protein level of the consequences of missense mutations in the human dystrophin rod domain. Our results suggest that it may participate in mechanical weakening of dystrophin-deficient muscle.
Organic Letters | 2009
Béatrice Legouin; Philippe Uriac; Sophie Tomasi; Loı̈c Toupet; Arnaud Bondon; Pierre van de Weghe
A new chiral molecular tweezer was synthesized with (1R,2R)-1,2-diaminocyclohexane as spacer and two molecules of (+)-usnic acid as pincers. The ability of this molecular tweezer to bind 2,4,7-trinitrofluorenone was studied. A charge-transfer complex was formed in which TNF was sandwiched between the two usnic acid units with pi-pi-stacked aromatic interactions.
Biochimica et Biophysica Acta | 2008
Sébastien Legardinier; Jean-François Hubert; Olivier Le Bihan; Christophe Tascon; Chantal Rocher; Céline Raguénès-Nicol; Arnaud Bondon; Serge Hardy; Elisabeth Le Rumeur
Dystrophin is a muscle scaffolding protein that establishes a structural link between the cytoskeleton and the extracellular matrix. Despite the large body of knowledge about the dystrophin gene and its interactions, the functional importance of the large central rod domain remains highly controversial. It is composed of 24 spectrin-like repeats interrupted by four hinges that delineate three sub-domains. We express repeat 1-3 and repeat 20-24 sub-domains, delineated by hinges 1-2 and 3-4 and the single repeats 2 and 23. We determine their lipid-binding properties, thermal and urea stabilities and refolding velocities. By using intrinsic tryptophan fluorescence spectroscopy and size exclusion chromatography, we show that repeat 2 and the repeat 1-3 sub-domain strongly interact with anionic lipids. By contrast, repeat 23 and the repeat 20-24 sub-domain do not interact with lipids. In addition, the repeat 1-3 sub-domain and repeat 2 are dramatically less stable and refold faster than the repeat 20-24 sub-domain and repeat 23. The contrasting properties of the two sub-domains clearly indicate that they make up two units of the rod domain that are not structurally interchangeable, thus providing molecular evidence supporting the observations on the biological function of dystrophin.
Tetrahedron-asymmetry | 1999
Erwan Galardon; Paul Le Maux; Arnaud Bondon; Gérard Simonneaux
Abstract The synthesis of a (carbonyl) (valine methyl ester) ruthenium(II) picket-fence complex bearing optically active α-methoxy-α(trifluoromethyl)phenylacetyl residues on both sides of the porphyrin plane (α,β,α,β-isomer) is described. For various amino esters, chiral recognition was observed for the complexation of the ligand with up to 52% enantiomeric excess for tert -leucine methyl ester. The dissociation rate constants of the two enantiomers of valine methyl ester were determined by 1 H NMR using magnetization transfer experiments, showing that the origin of the enantioselectivity in favour of the ( l )-valine (ca. 2.6:1) resides in the difference between the kinetics of the axial ligand dissociation of the two enantiomers.
Journal of Natural Products | 2013
Marieke Vansteelandt; Elodie Blanchet; Maxim Egorov; Fabien Petit; Loïc Toupet; Arnaud Bondon; Fabrice Monteau; Bruno Le Bizec; O. Thomas; Yves François Pouchus; Ronan Le Bot; Olivier Grovel
A new chlorinated sesquiterpenoid analogue of fumagillin, ligerin (1), was isolated from a marine-derived strain of Penicillium, belonging to the subgenus Penicillium, along with the known compounds penicillic acid (2), orcinol, and orsellinic acid. Chemical structures were established by an interpretation of spectroscopic data including IR, UV, and HRESIMS, together with analyses of 1D and 2D NMR spectra and X-ray analysis for the determination of the absolute configuration. Ligerin (1) displayed strong inhibitory activity against an osteosarcoma cell line. This is the first report of the isolation of a fumagillin analogue from a marine-derived Penicillium strain.
Journal of Medicinal Chemistry | 2012
Mathieu Laurencin; Baptiste Legrand; Emilie Duval; Joël Henry; Michèle Baudy-Floc'h; Céline Zatylny-Gaudin; Arnaud Bondon
Incorporation of aza-β(3)-amino acids into an endogenous neuropeptide from mollusks (ALSGDAFLRF-NH(2)) with weak antimicrobial activity allows the design of new AMPs sequences. Depending on the nature of the substitution, this can render the pseudopeptides inactive or lead to a drastic enhancement of the antimicrobial activity without high cytotoxicity. Structural studies of the pseudopeptides carried out by NMR and circular dichroism show the impact of aza-β(3)-amino acids on peptide structure. The first three-dimensional structures of pseudopeptides containing aza-β(3)-amino acids in aqueous micellar SDS were determined and demonstrate that the hydrazino turn can be formed in aqueous solution. Thus, AMP activity can be modulated through structural modifications induced by the nature and the position of such amino acid analogues in the peptide sequences.
European Biophysics Journal | 2007
Grégory Da Costa; Liza Mouret; Soizic Chevance; Elisabeth Le Rumeur; Arnaud Bondon
Detailed characterization of protein, peptide or drug interactions with natural membrane is still a challenge. This review focuses on the use of nuclear magnetic resonance (NMR) for the analysis of interaction of molecules with small unilamellar vesicles (SUV). These phospholipid vesicles are often used as model membranes for fluorescence or circular dichroism experiments. The various NMR approaches for studying molecule-lipid association are reviewed. After a brief survey of the SUV characterization, the use of heteronuclear NMR (phosphorous, carbon, fluorine) is described. Applications of proton NMR through transferred nuclear Overhauser effect to perform structural determination of peptide are presented. Special care is finally given to the influence of the kinetic of the interactions for the proton NMR of bound molecules in SUV, which can constitute a good model for the study of dynamical processes at the membrane surface.
European Journal of Inorganic Chemistry | 2000
Emmanuel Porhiel; Arnaud Bondon; Jacques Leroy
The synthesis and characterization of manganese complexes of β-octafluoro-meso-tetraarylporphyrins are reported. The presence of the electron-withdrawing β-fluorine atoms induces a very large shift of the redox potential for the oxidation of the manganese(II) derivatives. With the meso-aryl group bearing two ortho-chlorine atoms (2,6-dichlorophenyl) or five fluorine atoms (pentafluorophenyl), metal complexation leads to the isolation of pure manganese(II) compounds. The stability and catalytic activity of these new derivatives have been studied using hydrogen peroxide and iodosylbenzene as oxidants, and standard substrates for epoxidation and hydroxylation reactions. The results are compared to those obtained with the β-hydrogenated analogs under the same conditions. In the case of hydrogen peroxide, the high level of porphyrin degradation prevents efficient catalytic activity. With iodosylbenzene as oxidant, both stability and epoxidation are similar to those of the β-hydrogenated porphyrins, however, a substantial improvement in the efficiency of the hydroxylation of cyclohexane is observed with up to 33 turnovers with (perfluorotetraphenylporphyrin)manganese(II).