Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies.
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| Title: | Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies. |
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| Authors: | Harding, Benjamin D.1, Dixit, Gunjan1, Burridge, Kevin M.1, Sahu, Indra D.1, Dabney-Smith, Carole1, Edelmann, Richard E.1, Konkolewicz, Dominik1 d.konkolewicz@miamioh.edu, Lorigan, Gary A.1 gary.lorigan@miamioh.edu |
| Source: | Chemistry & Physics of Lipids. Jan2019, Vol. 218, p65-72. 8p. |
| Subjects: | Membrane proteins, Styrene, Maleic acid, Copolymers, Bilayer lipid membranes, Protein structure, Polymerization |
| Abstract: | Highlights • The size of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) were characterized using Dynamic Light Scattering. • EPR spectra showed the incorporation of a membrane protein into the nanoparticles and liposomes. • TEM images show the size and distribution of the SMALPs. Abstract Membrane proteins play an important role in maintaining the structure and physiology of an organism. Despite their significance, spectroscopic studies involving membrane proteins remain challenging due to the difficulties in mimicking their native lipid bilayer environment. Membrane mimetic systems such as detergent micelles, liposomes, bicelles, nanodiscs, lipodisqs have improved the solubility and folding properties of the membrane proteins for structural studies, however, each mimetic system suffers from its own limitations. In this study, using three different lipid environments, vesicles were titrated with styrene-maleic acid (StMA) copolymer leading to a homogeneous SMALP system (∼10 nm) at a weight ratio of 1:1.5 (vesicle: StMA solution). A combination of Dynamic Light Scattering (DLS) and Transmission Electron Microscopy (TEM) was used to characterize these SMALPs. We used a controlled synthesis mechanism to synthesize StMA based block copolymers called reversible addition-fragmentation chain transfer polymerization (RAFT) SMALPs. Incorporation of the Voltage Sensor Domain of KCNQ1 (Q1-VSD) into RAFT SMALPs indicates that this is a promising application of this system to study membrane proteins using different biophysical techniques. V165C in Q1-VSD corresponding to the hydrophobic region was incorporated into the SMALP system. Continuous Wave-Electron Paramagnetic Resonance (CW-EPR) line shape analysis showed line shape broadening, exposing a lower rigid component and a faster component of the spin label. [ABSTRACT FROM AUTHOR] |
| Copyright of Chemistry & Physics of Lipids is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
| Database: | Engineering Source |
| FullText | Text: Availability: 0 |
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| Header | DbId: egs DbLabel: Engineering Source An: 134274094 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Harding%2C+Benjamin+D%2E%22">Harding, Benjamin D.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Dixit%2C+Gunjan%22">Dixit, Gunjan</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Burridge%2C+Kevin+M%2E%22">Burridge, Kevin M.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Sahu%2C+Indra+D%2E%22">Sahu, Indra D.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Dabney-Smith%2C+Carole%22">Dabney-Smith, Carole</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Edelmann%2C+Richard+E%2E%22">Edelmann, Richard E.</searchLink><relatesTo>1</relatesTo><br /><searchLink fieldCode="AR" term="%22Konkolewicz%2C+Dominik%22">Konkolewicz, Dominik</searchLink><relatesTo>1</relatesTo><i> d.konkolewicz@miamioh.edu</i><br /><searchLink fieldCode="AR" term="%22Lorigan%2C+Gary+A%2E%22">Lorigan, Gary A.</searchLink><relatesTo>1</relatesTo><i> gary.lorigan@miamioh.edu</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Chemistry+%26+Physics+of+Lipids%22">Chemistry & Physics of Lipids</searchLink>. Jan2019, Vol. 218, p65-72. 8p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Membrane+proteins%22">Membrane proteins</searchLink><br /><searchLink fieldCode="DE" term="%22Styrene%22">Styrene</searchLink><br /><searchLink fieldCode="DE" term="%22Maleic+acid%22">Maleic acid</searchLink><br /><searchLink fieldCode="DE" term="%22Copolymers%22">Copolymers</searchLink><br /><searchLink fieldCode="DE" term="%22Bilayer+lipid+membranes%22">Bilayer lipid membranes</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+structure%22">Protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Polymerization%22">Polymerization</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Highlights • The size of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) were characterized using Dynamic Light Scattering. • EPR spectra showed the incorporation of a membrane protein into the nanoparticles and liposomes. • TEM images show the size and distribution of the SMALPs. Abstract Membrane proteins play an important role in maintaining the structure and physiology of an organism. Despite their significance, spectroscopic studies involving membrane proteins remain challenging due to the difficulties in mimicking their native lipid bilayer environment. Membrane mimetic systems such as detergent micelles, liposomes, bicelles, nanodiscs, lipodisqs have improved the solubility and folding properties of the membrane proteins for structural studies, however, each mimetic system suffers from its own limitations. In this study, using three different lipid environments, vesicles were titrated with styrene-maleic acid (StMA) copolymer leading to a homogeneous SMALP system (∼10 nm) at a weight ratio of 1:1.5 (vesicle: StMA solution). A combination of Dynamic Light Scattering (DLS) and Transmission Electron Microscopy (TEM) was used to characterize these SMALPs. We used a controlled synthesis mechanism to synthesize StMA based block copolymers called reversible addition-fragmentation chain transfer polymerization (RAFT) SMALPs. Incorporation of the Voltage Sensor Domain of KCNQ1 (Q1-VSD) into RAFT SMALPs indicates that this is a promising application of this system to study membrane proteins using different biophysical techniques. V165C in Q1-VSD corresponding to the hydrophobic region was incorporated into the SMALP system. Continuous Wave-Electron Paramagnetic Resonance (CW-EPR) line shape analysis showed line shape broadening, exposing a lower rigid component and a faster component of the spin label. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Chemistry & Physics of Lipids is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1016/j.chemphyslip.2018.12.002 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 8 StartPage: 65 Subjects: – SubjectFull: Membrane proteins Type: general – SubjectFull: Styrene Type: general – SubjectFull: Maleic acid Type: general – SubjectFull: Copolymers Type: general – SubjectFull: Bilayer lipid membranes Type: general – SubjectFull: Protein structure Type: general – SubjectFull: Polymerization Type: general Titles: – TitleFull: Characterizing the structure of styrene-maleic acid copolymer-lipid nanoparticles (SMALPs) using RAFT polymerization for membrane protein spectroscopic studies. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Harding, Benjamin D. – PersonEntity: Name: NameFull: Dixit, Gunjan – PersonEntity: Name: NameFull: Burridge, Kevin M. – PersonEntity: Name: NameFull: Sahu, Indra D. – PersonEntity: Name: NameFull: Dabney-Smith, Carole – PersonEntity: Name: NameFull: Edelmann, Richard E. – PersonEntity: Name: NameFull: Konkolewicz, Dominik – PersonEntity: Name: NameFull: Lorigan, Gary A. IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 01 Text: Jan2019 Type: published Y: 2019 Identifiers: – Type: issn-print Value: 00093084 Numbering: – Type: volume Value: 218 Titles: – TitleFull: Chemistry & Physics of Lipids Type: main |
| ResultId | 1 |
