Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
Identifieur interne : 001A42 ( Istex/Curation ); précédent : 001A41; suivant : 001A43Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
Auteurs : I. G. Denisov [États-Unis] ; Y. V. Grinkova [États-Unis] ; A. A. Lazarides [États-Unis] ; S. G. Sligar [États-Unis]Source :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2004.
Abstract
Using a recently described self-assembly process (Bayburt, T. H.; Grinkova, Y. V.; Sligar, S. G. Nano Letters 2002, 2, 853−856), we prepared soluble monodisperse discoidal lipid/protein particles with controlled size and composition, termed Nanodiscs, in which the fragment of dipalmitoylphosphatidylcholine (DPPC) bilayer is surrounded by a helical protein belt. We have customized the size of these particles by changing the length of the amphipathic helical part of this belt, termed membrane scaffold protein (MSP). Herein we describe the design of extended and truncated MSPs, the optimization of self-assembly for each of these proteins, and the structure and composition of the resulting Nanodiscs. We show that the length of the protein helix surrounding the lipid part of a Nanodisc determines the particle diameter, as measured by HPLC and small-angle X-ray scattering (SAXS). Using different scaffold proteins, we obtained Nanodiscs with the average size from 9.5 to 12.8 nm with a very narrow size distribution (±3%). Functionalization of the N-terminus of the scaffold protein does not perturb their ability to form homogeneous discoidal structures. Detailed analysis of the solution scattering confirms the presence of a lipid bilayer of 5.5 nm thickness in Nanodiscs of different sizes. The results of this study provide an important structural characterization of self-assembled phospholipid bilayers and establish a framework for the design of soluble amphiphilic nanoparticles of controlled size.
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DOI: 10.1021/ja0393574
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Nanodiscs with Controlled Size</title><author><name sortKey="Denisov, I G" sort="Denisov, I G" uniqKey="Denisov I" first="I. G." last="Denisov">I. G. Denisov</name><affiliation wicri:level="2"><mods:affiliation>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham, North Carolina 27708</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham</wicri:cityArea></affiliation><affiliation><mods:affiliation> Department of Biochemistry, University of Illinois.</mods:affiliation></affiliation><affiliation><mods:affiliation> Beckman Institute, University of Illinois.</mods:affiliation></affiliation></author><author><name sortKey="Grinkova, Y V" sort="Grinkova, Y V" uniqKey="Grinkova Y" first="Y. V." last="Grinkova">Y. V. Grinkova</name><affiliation wicri:level="2"><mods:affiliation>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham, North Carolina 27708</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham</wicri:cityArea></affiliation><affiliation><mods:affiliation> Department of Biochemistry, University of Illinois.</mods:affiliation></affiliation><affiliation><mods:affiliation> Beckman Institute, University of Illinois.</mods:affiliation></affiliation></author><author><name sortKey="Lazarides, A A" sort="Lazarides, A A" uniqKey="Lazarides A" first="A. A." last="Lazarides">A. A. Lazarides</name><affiliation wicri:level="2"><mods:affiliation>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham, North Carolina 27708</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham</wicri:cityArea></affiliation><affiliation><mods:affiliation> Duke University.</mods:affiliation></affiliation></author><author><name sortKey="Sligar, S G" sort="Sligar, S G" uniqKey="Sligar S" first="S. G." last="Sligar">S. G. Sligar</name><affiliation wicri:level="2"><mods:affiliation>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham, North Carolina 27708</mods:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>Contribution from the Departments of Biochemistry and Chemistry and the Beckman Institute,University of Illinois, Urbana, Illinois 61801, and Department of Mechanical Engineering andMaterials Science, Duke University, Durham</wicri:cityArea></affiliation><affiliation><mods:affiliation> Department of Biochemistry, University of Illinois.</mods:affiliation></affiliation><affiliation><mods:affiliation> Beckman Institute, University of Illinois.</mods:affiliation></affiliation><affiliation><mods:affiliation> Department of Chemistry, University of Illinois.</mods:affiliation></affiliation><affiliation><mods:affiliation> Corresponding author.</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Journal of the American Chemical Society</title><title level="j" type="abbrev">J. Am. Chem. Soc.</title><idno type="ISSN">0002-7863</idno><idno type="eISSN">1520-5126</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published">2004</date><date type="published">2004</date><biblScope unit="vol">126</biblScope><biblScope unit="issue">11</biblScope><biblScope unit="page" from="3477">3477</biblScope><biblScope unit="page" to="3487">3487</biblScope></imprint><idno type="ISSN">0002-7863</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0002-7863</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">Using a recently described self-assembly process (Bayburt, T. H.; Grinkova, Y. V.; Sligar, S. G. Nano Letters 2002, 2, 853−856), we prepared soluble monodisperse discoidal lipid/protein particles with controlled size and composition, termed Nanodiscs, in which the fragment of dipalmitoylphosphatidylcholine (DPPC) bilayer is surrounded by a helical protein belt. We have customized the size of these particles by changing the length of the amphipathic helical part of this belt, termed membrane scaffold protein (MSP). Herein we describe the design of extended and truncated MSPs, the optimization of self-assembly for each of these proteins, and the structure and composition of the resulting Nanodiscs. We show that the length of the protein helix surrounding the lipid part of a Nanodisc determines the particle diameter, as measured by HPLC and small-angle X-ray scattering (SAXS). Using different scaffold proteins, we obtained Nanodiscs with the average size from 9.5 to 12.8 nm with a very narrow size distribution (±3%). Functionalization of the N-terminus of the scaffold protein does not perturb their ability to form homogeneous discoidal structures. Detailed analysis of the solution scattering confirms the presence of a lipid bilayer of 5.5 nm thickness in Nanodiscs of different sizes. The results of this study provide an important structural characterization of self-assembled phospholipid bilayers and establish a framework for the design of soluble amphiphilic nanoparticles of controlled size.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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