Výsledky vyhledávání

Synthesis, Characterization and Applications of a Perdeuterated Amphipol

Autor: Fabrice Giusti, Laurent Catoire, Shuo Qian, Thomas G. Watkinson, J.-L. Popot, Marina Casiraghi, Jutta Rieger, Antonio N. Calabrese, Sheena E. Radford, Alison E. Ashcroft

Publikováno v: Journal of Membrane Biology
Journal of Membrane Biology, Springer Verlag (Germany), 2014, 247 (9-10), pp.909-924. ⟨10.1007/s00232-014-9656-x⟩
The Journal of Membrane Biology
The Journal of Membrane Biology, 2014, 247 (9-10), pp.909--924. ⟨10.1007/s00232-014-9656-x⟩
Journal of Membrane Biology, 2014, 247 (9-10), pp.909-924. ⟨10.1007/s00232-014-9656-x⟩

Amphipols are short amphipathic polymers that can substitute for detergents at the hydrophobic surface of membrane proteins (MPs), keeping them soluble in the absence of detergents while stabilizing them. The most widely used amphipol, known as A8-35

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::071056c568f627155eee8c087e92ed3e
https://hal.archives-ouvertes.fr/hal-02324075

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Thermal Fluctuations in Amphipol A8-35 Particles: A Neutron Scattering and Molecular Dynamics Study

Autor: Moeava Tehei, Giuseppe Zaccai, J.-L. Popot, Jonathan N. Sachs, Jason D. Perlmutter, Fabrice Giusti

Publikováno v: Journal of Membrane Biology
Journal of Membrane Biology, Springer Verlag (Germany), 2014, 247 (9-10), pp.897-908. ⟨10.1007/s00232-014-9725-1⟩
Journal of Membrane Biology, 2014, 247 (9-10), pp.897-908. ⟨10.1007/s00232-014-9725-1⟩
Journal of Membrane Biology, Springer Verlag (Germany), 2014, 247 (9-10), pp.897-908

Amphipols are a class of polymeric surfactants that can stabilize membrane proteins in aqueous solutions as compared to detergents. A8-35, the best-characterized amphipol to date, is composed of a polyacrylate backbone with ~35% of the carboxylates f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90f507565ff6642024f77e76aaabc6cf
https://hal.archives-ouvertes.fr/hal-02323382

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Nanoparticle surface-enhanced Raman scattering of bacteriorhodopsin stabilized by amphipol A8-35

Autor: Ekaterina Round, P. Utrobin, Taras Balandin, Valentin Gordeliy, Vitaly Polovinkin, Dieter Willbold, J.-L. Popot, Antoine Royant, Grigory Arzumanyan, Vladimir Chupin, O. Volkov, Valentin Borshchevskiy, D. von Stetten

Publikováno v: Journal of Membrane Biology
Journal of Membrane Biology, Springer Verlag (Germany), 2014, 247 (9-10), pp.971-80
Journal of Membrane Biology, 2014, 247 (9-10), pp.971-80

International audience; Surface-enhanced Raman spectroscopy (SERS) has developed dramatically since its discovery in the 1970s, because of its power as an analytical tool for selective sensing of molecules adsorbed onto noble metal nanoparticles (NPs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::083667406e6216913e365c983ed5c081
https://hal.univ-grenoble-alpes.fr/hal-01130634

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In vivo characterization of the biodistribution profile of amphipol A8-35

Autor: Dominique Bagnard, C. Le Bon, Fabrice Giusti, Nadège Baumlin, Aurore Fernandez, Gérard Crémel, J.-L. Popot

Publikováno v: The Journal of membrane biology. 247(9-10)

Amphipols (APols) are polymeric surfactants that keep membrane proteins (MPs) water-soluble in the absence of detergent, while stabilizing them. They can be used to deliver MPs and other hydrophobic molecules in vivo for therapeutic purposes, e.g., v

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98edba349f459408d81ea9916c268081
https://pubmed.ncbi.nlm.nih.gov/24898094

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High-resolution structure of a membrane protein transferred from amphipol to a lipidic mesophase

Autor: V. Schevchenko, Alexander Popov, Ivan Gushchin, Alexey Mishin, Vitaly Polovinkin, Taras Balandin, Vladimir Chupin, M. Sintsov, P. Utrobin, Ekaterina Round, Dieter Willbold, P. Chervakov, J.-L. Popot, Valentin Gordeliy, Alexander I. Kuklin, Valentin Borshchevskiy

Publikováno v: The Journal of membrane biology. 247(9-10)

Amphipols (APols) have become important tools for the stabilization, folding, and in vitro structural and functional studies of membrane proteins (MPs). Direct crystallization of MPs solubilized in APols would be of high importance for structural bio

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55f5986b4f4d234585ba4660349350d9
https://pubmed.ncbi.nlm.nih.gov/28229180

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Molecular dynamics simulations of a membrane protein/amphipol complex

Autor: J.-L. Popot, Jonathan N. Sachs, Jason D. Perlmutter

Publikováno v: The Journal of membrane biology. 247(9-10)

Amphipathic polymers known as “amphipols” provide a highly stabilizing environment for handling membrane proteins in aqueous solutions. A8-35, an amphipol with a polyacrylate backbone and hydrophobic grafts, has been extensively characterized and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29332f0786f8dc2f16e431b71c985a28
https://pubmed.ncbi.nlm.nih.gov/24930025

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Interaction of Amphipols with Sarcoplasmic Reticulum Ca2+-ATPase

Autor: Philippe Champeil, Thierry Menguy, Marc le Maire, Christophe Tribet, J.-L. Popot

Publikováno v: Journal of Biological Chemistry. 275:18623-18637

Amphipols are short-chain amphipathic polymers designed to keep membrane proteins soluble in aqueous solutions. We have evaluated the effects of the interaction of amphipols with sarcoplasmic reticulum Ca(2+)-ATPase either in a membrane-bound or a so

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1e64e4e26a3b4023adcdefee4817111
https://doi.org/10.1074/jbc.m000470200

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