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9 results on '"Nasiripourdori A"'

1. From Toxins Targeting Ligand Gated Ion Channels to Therapeutic Molecules

Author

Antoine Taly, Adak Nasiripourdori, Valérie Taly, and Thomas Grutter

Subjects
nAChR, P2X, GABA, Glycine, Serotonin, NMDA, AMPA, Kainate, Medicine
Abstract

Ligand-gated ion channels (LGIC) play a central role in inter-cellular communication. This key function has two consequences: (i) these receptor channels are major targets for drug discovery because of their potential involvement in numerous human brain diseases; (ii) they are often found to be the target of plant and animal toxins. Together this makes toxin/receptor interactions important to drug discovery projects. Therefore, toxins acting on LGIC are presented and their current/potential therapeutic uses highlighted.

Published
2011
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2. From Toxins Targeting Ligand Gated Ion Channels to Therapeutic Molecules

Author

Adak Nasiripourdori, Antoine Taly, Thomas Grutter, Valérie Taly, Department of Biology [Arak, Iran] (Faculty of Sciences), Arak University, Institut de Science et d'ingénierie supramoléculaires (ISIS), Réseau nanophotonique et optique, Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC)-Matériaux et nanosciences d'Alsace (FMNGE), Institut de Chimie du CNRS (INC)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA), Conception et application de molécules bioactives (CAMB), Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), TALY, Valerie, Université de Strasbourg (UNISTRA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Matériaux et Nanosciences Grand-Est (MNGE), Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Réseau nanophotonique et optique, and Université de Strasbourg (UNISTRA)-Université de Haute-Alsace (UHA) Mulhouse - Colmar (Université de Haute-Alsace (UHA))-Centre National de la Recherche Scientifique (CNRS)-Université de Strasbourg (UNISTRA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Models, Molecular, Serotonin, Health, Toxicology and Mutagenesis, [SDV]Life Sciences [q-bio], Glycine, lcsh:Medicine, AMPA receptor, Review, nAChR, Toxicology, 03 medical and health sciences, GABA, 0302 clinical medicine, Drug Discovery, AMPA, Animals, Humans, Receptor, Ion channel, 030304 developmental biology, Toxins, Biological, 0303 health sciences, Binding Sites, Dose-Response Relationship, Drug, Molecular Structure, Chemistry, Drug discovery, lcsh:R, Kainate, P2X, Ligand-Gated Ion Channels, Cell biology, [SDV] Life Sciences [q-bio], Biochemistry, NMDA, Ligand-gated ion channel, 030217 neurology & neurosurgery, Function (biology), Protein Binding
Abstract

International audience; Ligand-gated ion channels (LGIC) play a central role in inter-cellular communication. This key function has two consequences: (i) these receptor channels are major targets for drug discovery because of their potential involvement in numerous human brain diseases; (ii) they are often found to be the target of plant and animal toxins. Together this makes toxin/receptor interactions important to drug discovery projects. Therefore, toxins acting on LGIC are presented and their current/potential therapeutic uses highlighted.

Published
2011

3. Binding of long-chain α-neurotoxin would stabilize the resting state of nAChR: A comparative study with α-conotoxin

Author

Hossein Naderi-Manesh, Bijan Ranjbar, and Adak Nasiripourdori

Subjects
Models, Molecular, Neurotoxins, Health Informatics, Plasma protein binding, Receptors, Nicotinic, Torpedo, lcsh:Computer applications to medicine. Medical informatics, complex mixtures, law.invention, law, Modelling and Simulation, Animals, Neurotoxin, Conotoxin, lcsh:QH301-705.5, α conotoxin, Resting state fMRI, Chemistry, Research, Nicotinic acetylcholine receptor, Biochemistry, nervous system, lcsh:Biology (General), Modeling and Simulation, lcsh:R858-859.7, sense organs, Conotoxins, Long chain, Protein Binding
Abstract

Background The details of interaction in a complex between potent antagonists such as long chain α-neurotoxins and α-conotoxins with nicotinic acetylcholine receptor (nAChR), and conformational changes induced by these antagonists, are not yet clear. Modeling In order to uncover some of these critical structural features, we conducted a docking simulation and a molecular dynamics simulation (MD) of a model of the ligand binding domain of nAChR in complex with a long-chain α-neurotoxin and an α-conotoxin. Results Our docking results confirm the claim that T.nAChR is in the basal or resting state, which favors binding to the alpha-neurotoxins. Moreover, more correct "hits" for the α/γ interface upon docking for conotoxin-nAChR confirm the preference of conotoxin GI for the α/γ interface. More importantly, upon binding of α-neurotoxin, ligand-bonded nAChR is less dynamic in certain domains than the apo form of the conotoxin-AChR complex. Some critical interactions in the binding site such as the salt bridge formed between K145/D200 in the neurotoxin-nAChR complex is further stabilized during the MD simulation, while it is obviously more labile in the apo form. Conclusion These observations could support the claim that alpha neurotoxins stabilize the nAChR resting state.

Published
2009

4. Binding site locations and interaction of the isolated middle loop of snake neurotoxin I with muscle type nicotinic acetylcholine receptor: molecular dynamics and docking simulation study

Author

Hossein Naderi-Manesh, Bijan Ranjbar, and Adak Nasiripourdori

Subjects
Applied Mathematics, Muscle type, Biology, Bioinformatics, Computer Science Applications, Molecular dynamics, Nicotinic acetylcholine receptor, Structural Biology, Docking (molecular), Modelling and Simulation, Modeling and Simulation, Biophysics, Neurotoxin, Binding site, Molecular Biology
Published
2007

9. Binding of long-chain alpha-neurotoxin would stabilize the resting state of nAChR: a comparative study with alpha-conotoxin.

Author

Nasiripourdori A, Ranjbar B, and Naderi-Manesh H

Subjects
Animals, Conotoxins chemistry, Models, Molecular, Neurotoxins chemistry, Protein Binding, Receptors, Nicotinic chemistry, Torpedo, Conotoxins metabolism, Neurotoxins metabolism, Receptors, Nicotinic metabolism
Abstract

Background: The details of interaction in a complex between potent antagonists such as long chain alpha-neurotoxins and alpha-conotoxins with nicotinic acetylcholine receptor (nAChR), and conformational changes induced by these antagonists, are not yet clear. MODELING: In order to uncover some of these critical structural features, we conducted a docking simulation and a molecular dynamics simulation (MD) of a model of the ligand binding domain of nAChR in complex with a long-chain alpha-neurotoxin and an alpha-conotoxin., Results: Our docking results confirm the claim that T.nAChR is in the basal or resting state, which favors binding to the alpha-neurotoxins. Moreover, more correct "hits" for the alpha/gamma interface upon docking for conotoxin-nAChR confirm the preference of conotoxin GI for the alpha/gamma interface. More importantly, upon binding of alpha-neurotoxin, ligand-bonded nAChR is less dynamic in certain domains than the apo form of the conotoxin-AChR complex. Some critical interactions in the binding site such as the salt bridge formed between K145/D200 in the neurotoxin-nAChR complex is further stabilized during the MD simulation, while it is obviously more labile in the apo form., Conclusion: These observations could support the claim that alpha neurotoxins stabilize the nAChR resting state.

Published
2009
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