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4 results on '"Daniel Best"'

1. Probing the side chain tolerance for inhibitors of the CD95/PLCγ1 interaction

Author

Patrick Legembre, Ha Thanh Nguyen, Jean-Philippe Guégan, Pierre van de Weghe, Nicolas Levoin, Daniel Best, Mickael Jean, Chemistry, Oncogenesis, Stress and Signaling (COSS), Université de Rennes (UR)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de recherche en santé, environnement et travail (Irset), Université d'Angers (UA)-Université de Rennes (UR)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Bioprojet-Biotech, Institut des Sciences Chimiques de Rennes (ISCR), Université de Rennes (UR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), Institut National des Sciences Appliquées (INSA)-Institut National des Sciences Appliquées (INSA)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Institut National Du Cancer, Ligue Contre le Cancer, Fondation ARC pour la Recherche sur le Cancer, Agence Nationale de la Recherche, Institut National de la Santé et de la Recherche Médicale (INSERM)-CRLCC Eugène Marquis (CRLCC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Université d'Angers (UA)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-École des Hautes Études en Santé Publique [EHESP] (EHESP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES)-Ecole Nationale Supérieure de Chimie de Rennes (ENSCR)-Institut National des Sciences Appliquées - Rennes (INSA Rennes), and Institut National des Sciences Appliquées (INSA)-Université de Rennes (UNIV-RENNES)-Institut National des Sciences Appliquées (INSA)

Subjects
Models, Molecular, Protein Conformation, Surface Properties, Peptidomimetic, Stereochemistry, [SDV]Life Sciences [q-bio], Static Electricity, Clinical Biochemistry, Druggability, Pharmaceutical Science, Lupus, Arginine, 01 natural sciences, Biochemistry, Protein–protein interaction, chemistry.chemical_compound, symbols.namesake, Drug Discovery, Side chain, Cell migration, Amino Acid Sequence, fas Receptor, Phospholipase, Molecular Biology, chemistry.chemical_classification, Phospholipase C gamma, 010405 organic chemistry, Hydrogen bond, Organic Chemistry, Hydrogen Bonding, Peptoid, Fas, 3. Good health, 0104 chemical sciences, Amino acid, 010404 medicinal & biomolecular chemistry, chemistry, Mutagenesis, symbols, CD95, Protein protein interaction, Thermodynamics, Molecular Medicine, van der Waals force, Hydrophobic and Hydrophilic Interactions, Aromatic, Protein Binding
Abstract

International audience; Proceeding our effort to study protein-protein interaction between the death receptor CD95 and phospholipase PLCγ1, we present in the current work chameleon-like traits of peptidomimetic inhibitors. Minute analysis of the interaction suggests that most of the binding energy relies on van der Waals contacts rather than more specific features, such as hydrogen bonds or salt bridges. The two most important positions of the peptoid for its interaction with PLCγ1 (Arg184 and Arg187) were modified to test this hypothesis. While Arg184 proves to be exchangeable for Trp, with no alteration in affinity, the nature of the amino acid replacing Arg187 is more dependent on its positive charge. However, affinity can be partially recovered by increasing van der Waals interactions. Overall, this study shows that for both positions, a subtle balance exists between hydrophobicity, surface contacts and affinity for CD95/PLCγ1, and provides information for the generation of new therapeutic compounds toward this druggable target.

Published
2019

2. Disrupting the CD95-PLC gamma 1 interaction prevents Th17-driven inflammation

Author

Patrick Blanco, Amanda Poissonnier, Nicolas Levoin, Patrick Legembre, Lucie Morere, Pierre van de Weghe, Guennadi Kozlov, Sophie Martin, Isabelle Douchet, Ha Thanh Nguyen, Estibaliz Lazaro, Daniel Best, Raphael Pineau, Melissa Thomas, Jean-Philippe Guégan, Mickael Jean, Thomas Ducret, Pierre Vacher, Florence Jouan, Kalle Gehring, CRLCC Eugène Marquis (CRLCC), Chemistry, Oncogenesis, Stress and Signaling (COSS), Institut National de la Santé et de la Recherche Médicale (INSERM)-CRLCC Eugène Marquis (CRLCC)-Université de Rennes 1 (UR1), Université de Rennes (UNIV-RENNES)-Université de Rennes (UNIV-RENNES), Bioprojet-Biotech, McGill University = Université McGill [Montréal, Canada], Composantes innées de la réponse immunitaire et différenciation (CIRID), Université Bordeaux Segalen - Bordeaux 2-Centre National de la Recherche Scientifique (CNRS), Hôpital Haut-Lévêque [CHU Bordeaux], CHU Bordeaux [Bordeaux], Université de Bordeaux (UB), Centre de recherche Cardio-Thoracique de Bordeaux [Bordeaux] (CRCTB), Université Bordeaux Segalen - Bordeaux 2-CHU Bordeaux [Bordeaux]-Institut National de la Santé et de la Recherche Médicale (INSERM), Actions for OnCogenesis understanding and Target Identification in ONcology (ACTION), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bordeaux Segalen - Bordeaux 2-Institut Bergonié [Bordeaux], UNICANCER-UNICANCER, INCa PLBIO, Ligue Contre le Cancer, Fondation ARC, ANR PRCE, Fondation Arthritis, Canadian Institutes of Health Research [FRN-156276], Université de Rennes (UR)-CRLCC Eugène Marquis (CRLCC)-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut Bergonié [Bordeaux], and UNICANCER-UNICANCER-Université Bordeaux Segalen - Bordeaux 2-Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
0301 basic medicine, Lupus erythematosus, biology, Chemistry, Peptidomimetic, Inflammation, [SDV.CAN]Life Sciences [q-bio]/Cancer, Cell Biology, Fas receptor, medicine.disease, 3. Good health, Cell biology, 03 medical and health sciences, 030104 developmental biology, biology.protein, medicine, HIV Protease Inhibitor, Ritonavir, FADD, medicine.symptom, Signal transduction, Molecular Biology, medicine.drug
Abstract

International audience; CD95L is a transmembrane ligand (m-CD95L) that is cleaved by metalloproteases to release a soluble ligand (s-CD95L). Unlike m-CD95L, interaction between s-CD95L and CD95 fails to recruit caspase-8 and FADD to trigger apoptosis and instead induces a Ca2+ response via docking of PLC gamma 1 to the calcium-inducing domain (CID) within CD95. This signaling pathway induces accumulation of inflammatory Th17 cells in damaged organs of lupus patients, thereby aggravating disease pathology. A large-scale screen revealed that the HIV protease inhibitor ritonavir is a potent disruptor of the CD95-PLC gamma 1 interaction. A structure-activity relationship approach highlighted that ritonavir is a peptidomimetic that shares structural characteristics with CID with respect to docking to PLC gamma 1. Thus, we synthesized CID peptidomimetics abrogating both the CD95-driven Ca2+ response and transmigration of Th17 cells. Injection of ritonavir and the CID peptidomimetic into lupus mice alleviated clinical symptoms, opening a new avenue for the generation of drugs for lupus patients.

Published
2018

3. C-branched iminosugars: α-glucosidase inhibition by enantiomers of isoDMDP, isoDGDP, and isoDAB-L-isoDMDP compared to miglitol and miglustat

Author

Yves Blériot, Dominic S. Alonzi, A. Waldo Saville, Alexander C. Weymouth-Wilson, Francis Xavier Wilson, Sarah F. Jenkinson, Atsushi Kato, Daniel Best, George W. J. Fleet, Shinpei Nakagawa, Takahito Kunimatsu, Terry D. Butters, Caroline Norez, R. Fernando Martínez, Frédéric Becq, James Mui, Chemistry Research Laboratory, University of Oxford [Oxford], Oxford Glycobiology Institute, Department of Hospital Pharmacy [Toyama], University of Toyama, Institut de physiologie et biologie cellulaires (IPBC), Université de Poitiers-Centre National de la Recherche Scientifique (CNRS), Institut de Chimie des Milieux et Matériaux de Poitiers (IC2MP), Institut national des sciences de l'Univers (INSU - CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Poitiers-Institut de Chimie du CNRS (INC), Summit PLC, 91, DEXTRA Laboratories Ltd., The Science and Technology Centre, Synthèse Organique (E5), Université de Poitiers-Centre National de la Recherche Scientifique (CNRS)-Université de Poitiers-Centre National de la Recherche Scientifique (CNRS), Dextra Laboratories Ltd, and The Science and Technology Centre, Whiteknights Road, Reading, RG6 6BZ, U.K.

Subjects
1-Deoxynojirimycin, Stereochemistry, MESH: Biological Products, [SDV]Life Sciences [q-bio], Molecular Conformation, MESH: alpha-Glucosidases, Angiogenesis Inhibitors, 010402 general chemistry, 01 natural sciences, MESH: Dose-Response Relationship, Drug, chemistry.chemical_compound, Structure-Activity Relationship, MESH: Structure-Activity Relationship, Miglustat, medicine, Hydroxymethyl, Glycoside Hydrolase Inhibitors, Enzyme Inhibitors, ComputingMilieux_MISCELLANEOUS, MESH: Angiogenesis Inhibitors, Biological Products, MESH: Molecular Conformation, Dose-Response Relationship, Drug, 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Miglitol, Organic Chemistry, Stereoisomerism, alpha-Glucosidases, Maltose, [CHIM.CATA]Chemical Sciences/Catalysis, MESH: Stereoisomerism, Disaccharidase, 3. Good health, 0104 chemical sciences, Imino Sugars, MESH: Imino Sugars, chemistry, Biochemistry, MESH: Enzyme Inhibitors, Aldol condensation, Enantiomer, Maltase, [CHIM.OTHE]Chemical Sciences/Other, MESH: 1-Deoxynojirimycin, medicine.drug
Abstract

International audience; The Ho crossed aldol condensation provides access to a series of carbon branched iminosugars as exemplified by the synthesis of enantiomeric pairs of isoDMDP, isoDGDP, and isoDAB, allowing comparison of their biological activities with three linear isomeric natural products DMDP, DGDP, and DAB and their enantiomers. L-IsoDMDP [(2S,3S,4R)-2,4-bis(hydroxymethyl)pyrrolidine-3,4-diol], prepared in 11 steps in an overall yield of 45% from d-lyxonolactone, is a potent specific competitive inhibitor of gut disaccharidases [K(i) 0.081 μM for rat intestinal maltase] and is more effective in the suppression of hyperglycaemia in a maltose loading test than miglitol, a drug presently used in the treatment of late onset diabetes. The partial rescue of the defective F508del-CFTR function in CF-KM4 cells by L-isoDMDP is compared with miglustat and isoLAB in an approach to the treatment of cystic fibrosis.

Published
2013

4. Cystic fibrosis and diabetes: isoLAB and isoDAB, enantiomeric carbon-branched pyrrolidine iminosugars

Author

Yves Blériot, Dominic S. Alonzi, Terry D. Butters, A. Waldo Saville, Mark R. Wormald, Atsushi Kato, Daniel Best, Caroline Norez, Isao Adachi, Frédéric Becq, George W. J. Fleet, Sarah F. Jenkinson, Chemistry Research Laboratory [Oxford, UK], University of Oxford [Oxford], Oxford Glycobiology Institute, Institut de physiologie et biologie cellulaires (IPBC), Université de Poitiers-Centre National de la Recherche Scientifique (CNRS), Synthèse et réactivité des substances naturelles (SRSN), Université de Poitiers-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Department of Hospital Pharmacy [Toyama], and University of Toyama

Subjects
Stereochemistry, Glucosidase Inhibitor, Iminosugar, [CHIM.THER]Chemical Sciences/Medicinal Chemistry, 010402 general chemistry, 01 natural sciences, Biochemistry, Cystic fibrosis, [SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tract, Pyrrolidine, chemistry.chemical_compound, Glycogen phosphorylase, Drug Discovery, Ribose, medicine, [SDV.MHEP.PHY]Life Sciences [q-bio]/Human health and pathology/Tissues and Organs [q-bio.TO], 010405 organic chemistry, [CHIM.ORGA]Chemical Sciences/Organic chemistry, Organic Chemistry, medicine.disease, 0104 chemical sciences, Hexosaminidases, chemistry, [SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacology, Enantiomer
Abstract

Acetonides are the only protecting groups used in the syntheses of isoDAB from D -ribose and of isoLABfrom D -tagatose. isoDAB is a potent and highly specific competitive a -glucosidase inhibitor (for rice a -glucosidase, K i =4 l M for isoDAB compared to K i 14 M for DAB). isoDAB is not an—whereas DAB isa potent—inhibitor of glycogen phosphorylase. This is the first example of any potent inhibition of glyco-sidases by a carbon-branched iminosugar pyrrolidine. Although isoLAB shows no inhibition of any glyco-sidase, preliminary experiments suggest that isoLAB partially rescues the defective F508del-CFTRfunction and so may have a role in the study of cystic fibrosis. 2010 Elsevier Ltd. All rights reserved. Around200naturalproductsareknownthatmaybedescribedascarbohydratemimicsinwhichtheringoxygenofasugarisreplacedby nitrogen 1 —but all of them have linear carbon chains; modifica-tions of the analogous iminosugar have been developed to givesub-nanomolar inhibition of fucosidases, 2 hexosaminidases

Published
2010

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