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A Membrane-reconstituted Multisubunit Functional Proton Pump on Mesoporous Silica Particles
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för fysikalisk kemi, oorganisk kemi och strukturkemi.
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik.
2009 (Engelska)Ingår i: ACS Nano, ISSN 1936-0851, E-ISSN 1936-086X, Vol. 3, nr 9, s. 2639-2646Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

We have investigated formation of a proteolipid membrane surrounding mesoporous silica particles with a diameter of 550 nm and pore sizes of 3.0 nm. A multisubunit redox-driven proton pump, cytochrome c oxidase, was incorporated into the membrane and we show that the enzyme is fully functional, both with respect to catalysis of O2 reduction to water, and charge separation across the membrane. The orientation of cytochrome c oxidase in the membrane was found to be the same (~70/30 %) in the lipid vesicles and in the silica-particle supported lipid membrane, which provides information on the mechanism by which the vesicles adsorb to the surface. Furthermore, cytochrome c oxidase could maintain a proton electrochemical gradient across the supported proteomembrane, i.e. the membrane system was proton tight, defining an interior particle compartment that is separated from the surrounding aqueous media. Such a biofunctional cellular interface, supported onto a colloid that has a connected interior cytoskeleton-like pore structure, provides a basis for functional studies of membrane-bound transport proteins, and also for applications within pharmaceutical drug delivery.

Ort, förlag, år, upplaga, sidor
2009. Vol. 3, nr 9, s. 2639-2646
Nyckelord [en]
Supported lipid bilayer, mesoporous spheres, nanoparticles, membrane protein, drug delivery, cytochrome c oxidase
Nationell ämneskategori
Oorganisk kemi Industriell bioteknik Fysikalisk kemi
Forskningsämne
biokemi; materialvetenskap
Identifikatorer
URN: urn:nbn:se:su:diva-27829DOI: 10.1021/nn9005413ISI: 000269988600027OAI: oai:DiVA.org:su-27829DiVA, id: diva2:218562
Projekt
Synthesis, functionalisation and controlled release of mesoporous materialsTillgänglig från: 2009-05-20 Skapad: 2009-05-20 Senast uppdaterad: 2017-12-13Bibliografiskt granskad
Ingår i avhandling
1. Harnessing Mesoporous Spheres - transport studies and biotechnological applications
Öppna denna publikation i ny flik eller fönster >>Harnessing Mesoporous Spheres - transport studies and biotechnological applications
2009 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

Applications in controlled release and delivery calls for a good understanding of molecular transport within the carrier material and the dominating release mechanisms. It is clear that a better understanding of hindered transport and diffusion of guest molecules is important when developing new porous materials, e.g., surfactant templated silica spheres, for biotechnological applications. Confocal laser scanning microscopy was used to quantify the bulk release and intraparticle transport of small charged fluorescent dyes, and fluorescently-tagged neutral dextran, from mesoporous silica spheres. The time dependent release and the concentration profiles within the spheres have been used to analyze the release mechanisms using appropriate models. While the small, non-adsorbing anionic dye is released following a simple diffusion driven process, the concentration of the cationic dye varies radially within the spheres after loading. The release of the cationic dye is controlled by diffusion after an initial period of rapid release, which could be due to a significant fraction of the cationic dye that remains permanently attached to the negatively charged walls of the mesoporous silica spheres. The diffusion of dextran and the resulting flat concentration profiles could be related to the complex structural feature of the cylindrical pores close to the surface, and a possible conformational change of the dextran with the concentration. The stability and leaching of a catalytic enzyme, lipase, immobilized in hydrophobilized mesoporous support has also been quantified. Colloidal monodisperse mesoporous silica spheres were synthesized and transmission electron microscopy showed that the inner pore structure display a radially extending pores. The mesoporous spheres were used as solid supports for a lipid membrane incorporated with a multi-subunit redox-driven proton pump, which was shown to remain functional.

Ort, förlag, år, upplaga, sidor
Stockholm: Department of Physical, Inorganic and Structural Chemistry, Stockholm University, 2009. s. 69
Nyckelord
Mesoporous, spheres, particles, CLSM, TEM, controlled-release, molecular transport, lipid membrane, enzyme, intraparticle, lipase, solid support
Nationell ämneskategori
Oorganisk kemi
Forskningsämne
materialvetenskap
Identifikatorer
urn:nbn:se:su:diva-27797 (URN)978-91-7155-898-5 (ISBN)
Disputation
2009-09-02, Nordenskiöldsalen, Geovetenskapens hus, Svante Arrhenius väg 8 C, Stockholm, 10:00 (Engelska)
Opponent
Handledare
Projekt
Synthesis, functionalisation and controlled release of mesoporous materials
Tillgänglig från: 2009-05-27 Skapad: 2009-05-19 Senast uppdaterad: 2009-05-20Bibliografiskt granskad
2. Membrane-mimetic systems: Novel methods and results from studies of respiratory enzymes
Öppna denna publikation i ny flik eller fönster >>Membrane-mimetic systems: Novel methods and results from studies of respiratory enzymes
2013 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
Abstract [en]

The processes localized to biological membranes are of great interest, both from a scientific and pharmaceutical point of view. Understanding aspects such as the detailed mechanism and regulation of these processes requires investigation of the structure and function of the membrane-bound proteins in which they take place. The study of these processes is often complicated by the need to create in vitro systems that mimic the environment in which these proteins are normally found in vivo. This thesis describes some of the methods available for membrane-protein studies in membrane-mimetic systems, as well as our work aimed at developing such systems. Furthermore, results from studies using these systems are described.

In the first two studies, described in Papers I & II, we investigated the use of silica particle-supported lipid bilayers, both for membrane-protein studies and as possible drug-delivery vehicles. Successful reconstitution of a multisubunit proton-pump, cytochrome c oxidase is described and characterized. Initial attempts to develop drug-delivery systems with two different targeting peptides are also described in the thesis.

The second part of this thesis revolves around our work with membraneprotein dependent pathways. Results from studies of systems where the proton- pump bo3 oxidase and ATP synthase work in concert are described. The results show a surprising lipid-composition dependence for the coupled bo3- ATP-synthase activity (Paper III).

Finally, a new system utilizing synaptic vesicle-fusion proteins for coreconstitution of membrane proteins is described, showing successful coreconstitution of a small respiratory chain, delivery of soluble proteins to preformed liposomes and reconstitution of ATP synthase in native membranes (Paper IV).

Ort, förlag, år, upplaga, sidor
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2013. s. 55
Nyckelord
Lipids, membrane proteins, method development, respiration, reconstitution, supported membranes, SNAREs, liposome fusion, lipid-protein interactions
Nationell ämneskategori
Biokemi och molekylärbiologi
Forskningsämne
biokemi
Identifikatorer
urn:nbn:se:su:diva-94554 (URN)978-91-7447-774-0 (ISBN)
Disputation
2013-11-08, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (Engelska)
Opponent
Handledare
Anmärkning

At the time of the doctoral defense, the following papers were unpublished and had a status as follows: Paper 3: Manuscript. Paper 4: Manuscript.

Tillgänglig från: 2013-10-17 Skapad: 2013-10-04 Senast uppdaterad: 2013-10-10Bibliografiskt granskad

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Av författaren/redaktören
Nordlund, GustavNg, Jovice Boon SingBergström, LennartBrzezinski, Peter
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Institutionen för biokemi och biofysikInstitutionen för fysikalisk kemi, oorganisk kemi och strukturkemi
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ACS Nano
Oorganisk kemiIndustriell bioteknikFysikalisk kemi

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