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dc.contributor.authorAsmar-Rovira, Guillermo A.
dc.contributor.authorAsseo-García, Aloysha M.
dc.contributor.authorQuesada, Orestes
dc.contributor.authorHanson, Michael A.
dc.contributor.authorNogueras, Carlos
dc.contributor.authorLasalde-Dominicci, José A.
dc.contributor.authorC. Stevens, Raymond
dc.date.accessioned2017-05-31T21:02:42Z
dc.date.available2017-05-31T21:02:42Z
dc.date.copyrightAll of the material available from the PMC site is provided by the respective publishers or authors. Almost all of it is protected by U.S. and/or foreign copyright laws, even though PMC provides free access to it. (See Public Domain Material below, for one exception.) The respective copyright holders retain rights for reproduction, redistribution and reuse. Users of PMC are directly and solely responsible for compliance with copyright restrictions and are expected to adhere to the terms and conditions defined by the copyright holder. Transmission, reproduction, or reuse of protected material, beyond that allowed by the fair use principles of the copyright laws, requires the written permission of the copyright owners. U.S. fair use guidelines are available from the Copyright Office at the Library of Congress.en_US
dc.date.issued2009-05-01
dc.identifier.citationAsmar-Rovira, G. A., Asseo-García, A. M., Quesada, O., Hanson, M. A., Nogueras, C., Lasalde-Dominicci, J. A., & Stevens, R. C. (2008). Biophysical and ion channel functional characterization of the Torpedo californica nicotinic acetylcholine receptor in varying detergent-lipid environments. The Journal of Membrane Biology, 223(1), 13–26. http://doi.org/10.1007/s00232-008-9107-7en_US
dc.identifier.issn1432-1424
dc.identifier.urihttp://hdl.handle.net/11721/1623
dc.description.abstractThe nicotinic acetylcholine receptor (nAChR) of Torpedo electric rays has been extensively characterized over the last three decades. However, the molecular mechanisms by which detergents influence membrane protein stability and function remain poorly understood, and elucidation of the dynamic detergent-lipid-protein interactions of solubilized membrane proteins is a largely unexplored research field. This study examined nine detergents upon nAChR solubilization and purification, to assess receptor lipid composition using GC (Gas Chromatography)-FID (Flame Ionization) and/or GC-MSD (Mass Selective Detectors), stability and aggregation state using A-SEC (Analytical Size-Exclusion Chromatography) and EM (Electron Microscopy), and planar lipid bilayers to measure ion channel function. Detergent solubilization of nAChR-enriched membranes did not result in significant native lipid depletion or destabilization. Upon purification, native lipid depletion occurred in all detergents, with lipid-analog detergents [CHAPS (3-[(3-Cholamidopropyl)-dimethylammonio]-1-propane sulfonate), FC-12 (n-Dodecylphosphocholine) and sodium cholate (3α,7α,12α-Trihydroxy-5β-cholan-24-oic acid)] maintaining stability and supporting ion channel function, while non-lipid analog detergents [Cymal-6 (6-Cyclohexyl-1-hexyl-β-d-maltoside), DDM (n-Dodecyl-β-d-maltopyranoside), LDAO (Lauryldimethylamine-N-oxide) and OG (n-Octyl-β-d-glucopyranoside)] showed decreased stability and significant reduction or loss of ion channel function. Anapoe-C12E9 (Polyoxyethylene-(9)-dodecyl ether) and BigCHAP (N,N′-bis-(3-d-Gluconamidopropyl) cholamide) retained residual amounts of native lipid, maintaining moderate stability and ion channel function when compared to lipid-analog detergents. Overall, these results show that the nAChR can be stable and functional in lipid-analog detergents or in detergents that retain moderate amounts of residual native lipids, while the opposite is true about non-lipid analog detergents. These results highlight the importance of careful biophysical characterization of membrane proteins for future functional or structural studies in the detergent-solubilized state.en_US
dc.description.sponsorshipNIH (National Institutes of Health) grants R01GM056371, S06GM008102, SNRP U54NS043011 and UPR Institutional Funds for Research (to José A. Lasalde-Dominicci), the NIH-MBRS (Minority Biomedical Research Support) Research Initiative for Scientific Enhancement (RISE) grant R25GM061151 and the NIH Roadmap grant P50GM073197 (to Raymond C. Stevens) and Alliances for Graduate Education in the Professoriate (AGEP) and RISE fellowships (to Guillermo A. Asmar-Rovira).en_US
dc.Format.extent5.20 MBen_US
dc.language.isoen_USen_US
dc.publisherSpringer-Verlagen_US
dc.subjectnAChRen_US
dc.subjectFunctional characterizationen_US
dc.subjectPlanar lipid bilayersen_US
dc.subjectIntegral membrane proteinsen_US
dc.subjectDetergentsen_US
dc.subjectMembrane lipidsen_US
dc.subjectBiophysical characterizationen_US
dc.titleBiophysical and Ion Channel Functional Characterization of the Torpedo Californica Nicotinic Acetylcholine Receptor in Varying Detergent-Lipid Environmentsen_US
dc.typeArticleen_US
dc.rights.licenceArticles that are available through the PMC OAI and FTP services are still protected by copyright but are distributed under a Creative Commons or similar license that generally allows more liberal use than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all the articles.en_US
dcterms.licenseArticles that are available through the PMC OAI and FTP services are still protected by copyright but are distributed under a Creative Commons or similar license that generally allows more liberal use than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all the articles.en_US
dcterms.rightsThe respective copyright holders retain rights for reproduction, redistribution and reuse.en_US
dcterms.rightsHolderThe respective copyright holders retain rights for reproduction, redistribution and reuse. Users of PMC are directly and solely responsible for compliance with copyright restrictions and are expected to adhere to the terms and conditions defined by the copyright holder.en_US
dc.identifier.doiDOI: 10.1007/s00232-008-9107-7en_US
dc.local.DepartmentDepartment of Biologyen_US
dc.local.FacultyCollege of Natural Sciencesen_US
dc.contributor.campusUniversity of Puerto Rico, Río Piedras Campus


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Articles that are available through the PMC OAI and FTP services are still protected by copyright but are distributed under a Creative Commons or similar license that generally allows more liberal use than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all the articles.
Excepto si se señala otra cosa, la licencia del ítem se describe como Articles that are available through the PMC OAI and FTP services are still protected by copyright but are distributed under a Creative Commons or similar license that generally allows more liberal use than a traditional copyrighted work. Please refer to the license statement in each article for specific terms of use. The license terms are not identical for all the articles.