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Selective and atp driven transport of ions across supported membranes into nanoporous carriers using gramicidin a and atp synthase
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK), Materials Chemistry.
Stockholm University, Faculty of Science, Department of Materials and Environmental Chemistry (MMK).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2013 (English)In: Physical Chemistry, Chemical Physics - PCCP, ISSN 1463-9076, E-ISSN 1463-9084, Vol. 15, no 8, p. 2733-2740Article in journal (Refereed) Published
Abstract [en]

We report a robust and versatile membrane protein based system for selective uptake and release of ions from nanoporous particles sealed with ion-tight lipid bilayers of various compositions that is driven by the addition of ATP or a chemical potential gradient. We have successfully incorporated both a passive ion channel-type peptide (gramicidin A) and a more complex primary sodium ion transporter (ATP synthase) into the supported lipid bilayers on solid nanoporous silica particles. Protein-mediated controlled release/uptake of sodium ions across the ion-tight lipid bilayer seal from or into the nanoporous silica carrier was imaged in real time using a confocal laser scanning microscope and the intensity changes were quantified. ATP-driven transport of sodium ions across the supported lipid bilayer against a chemical gradient was demonstrated. The possibility of designing durable carriers with tight lipid membranes, containing membrane proteins for selective ion uptake and release, offers new possibilities for functional studies of single or cascading membrane protein systems and could also be used as biomimetic microreactors for controlled synthesis of inorganic multicomponent materials.

Place, publisher, year, edition, pages
2013. Vol. 15, no 8, p. 2733-2740
National Category
Chemical Sciences Physical Chemistry Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:su:diva-88325DOI: 10.1039/c2cp43166aISI: 000314365800014OAI: oai:DiVA.org:su-88325DiVA, id: diva2:611832
Funder
Swedish Research CouncilVinnovaThe Knowledge FoundationSwedish Foundation for Strategic Research
Note

AuthorCount:6;

Available from: 2013-03-19 Created: 2013-03-12 Last updated: 2022-02-24Bibliographically approved

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Mille, Christianvon Ballmoos, ChristophBergström, Lennart

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Department of Materials and Environmental Chemistry (MMK)Materials ChemistryDepartment of Biochemistry and Biophysics
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