Selective and ATP-driven transport of ions across supported membranes into nanoporous carriers using gramicidin A and ATP synthaseShow others and affiliations
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
Keywords [en]
Adenosine Triphosphate, ATP Synthetase Complexes, Fluorescein, Gramicidin, IodidesIon TransportIons, Lipid Bilayers, Nanopores, Silicon Dioxide, Sodium
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-27379DOI: 10.1039/c2cp43166aScopus ID: 2-s2.0-84873288866OAI: oai:DiVA.org:ri-27379DiVA, id: diva2:1054383
Note
A3078
2016-12-082016-12-082020-12-01Bibliographically approved