Lactobionamide Surfactants with Hydrogenated, Perfluorinated or Hemifluorinated Tails: Physical-Chemical and Biochemical Characterization
| Autor: | Bernard Pucci, Anne-Sylvie Fabiano, Christine Ebel, Nicolas Michel, Jean-Luc Popot, Cécile Breyton, Florence Lebaupain, Andrés G. Salvay, Grégory Durand, Blandine Olivier |
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| Přispěvatelé: | Physico-chimie moléculaire des membranes biologiques (PCMMB), Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7), Institut de biologie structurale (IBS - UMR 5075), Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Grenoble Alpes (UGA)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de Chimie Bioorganique et des Systèmes Moléculaires Vectoriels (LCBOSMV), Avignon Université (AU), Equipe Chimie Bioorganique et Systèmes Amphiphiles, Alcatel-Thalès III-V lab (III-V Lab), THALES-ALCATEL, European Project: 32853,IMPS, Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS), Institut de biologie structurale (IBS - UMR 5075 ), Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), THALES [France]-ALCATEL |
| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Chemical Phenomena
Biochemical Phenomena MESH: Molecular Structure MESH: Solutions Disaccharides 010402 general chemistry Biochemistry 01 natural sciences Micelle Surface-Active Agents 03 medical and health sciences Pulmonary surfactant Amphiphile MESH: Disaccharides Electrochemistry Molecule General Materials Science [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology MESH: Chemistry Physical MESH: Biochemical Phenomena Spectroscopy 030304 developmental biology 0303 health sciences Chromatography Aqueous solution Molecular Structure [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM] Chemistry Physical Chemistry MESH: Biochemistry MESH: Hydrogen MESH: Surface-Active Agents MESH: Chemical Phenomena Fluorine Surfaces and Interfaces Reversed-phase chromatography MESH: Fluorine Condensed Matter Physics 0104 chemical sciences Solutions [SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM] Membrane Chemical engineering Critical micelle concentration Hydrogen |
| Zdroj: | Langmuir Langmuir, American Chemical Society, 2006, 22 (21), pp.8881-8890. ⟨10.1021/la061083l⟩ Langmuir, American Chemical Society, 2006, 22, pp.8881-8890 Langmuir, 2006, 22 (21), pp.8881-8890. ⟨10.1021/la061083l⟩ |
| ISSN: | 0743-7463 1520-5827 |
| DOI: | 10.1021/la061083l⟩ |
| Popis: | International audience; Detergents are customarily used to solubilize cell membranes and keep membrane proteins soluble in aqueous buffers, but they often lead to irreversible protein inactivation. Hemifluorinated amphiphiles with hybrid hydrophobic chains have been specifically designed to minimize the denaturating propensity of surfactants toward membrane proteins. We have studied the physical-chemical and biochemical properties of lactobionamide surfactants bearing either a hydrogenated, a fluorinated or a hemifluorinated chain (respectively H-, F-, and HF-Lac). We show that the dual composition of the hydrophobic chain of HF-Lac endows it with unusual physical-chemical properties as regards its critical micellar concentration, interfacial area per molecule, and behavior upon reverse phase chromatography. Analytical ultracentrifugation shows that, whereas H-Lac assembles into well-defined micelles, F-Lac and HF-Lac form large and heterogeneous assemblies, whose size increases with surfactant concentration. Molecular dynamics calculations suggest that F-Lac forms cylindrical micelles. The ability of HF-Lac to keep membrane proteins soluble was examined using the cytochrome b(6) f complex from Chlamydomonas reinhardtii's chloroplast as a model protein. HF-Lac/b(6) f complexes form particles relatively homogeneous in size, in which the b(6) f complex is as stable or markedly more stable, depending on the surfactant concentration, than it is in equivalent concentrations of hydrogenated surfactants, including H-Lac. |
| Databáze: | OpenAIRE |
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