Evaluation of DIBMA nanoparticles of variable size and anionic lipid content as tools for the structural and functional study of membrane proteins

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dc.contributor.authorVoskoboynikova, Natalia
dc.contributor.authorMargheritis, Eleonora Germana
dc.contributor.authorKodde, Felix
dc.contributor.authorRademacher, Malte
dc.contributor.authorSchowe, Maurice
dc.contributor.authorBudke-Gieseking, Annette
dc.contributor.authorPsathaki, Olympia-Ekaterini
dc.contributor.authorSteinhoff, Heinz-Jurgen
dc.contributor.authorCosentino, Katia
dc.date.accessioned2021-12-23T15:57:51Z-
dc.date.available2021-12-23T15:57:51Z-
dc.date.issued2021
dc.identifier.issn00052736
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/3177-
dc.description.abstractAmphiphilic maleic acid-containing polymers allow for the direct extraction of membrane proteins into stable, homogenous, water-soluble copolymer/lipid nanoparticles without the use of detergents. By adjusting the polymer/lipid ratio, the size of the nanoparticles can be tuned at convenience for the incorporation of protein complexes of different size. However, an increase in the size of the lipid nanoparticles may correlate with increased sample heterogeneity, thus hampering their application to spectroscopic and structural techniques where highly homogeneous samples are desirable. In addition, size homogeneity can be affected by low liposome solubilization efficiency by DIBMA, which carries a negative charge, in the presence of high lipid charge density. In this work, we apply biophysical tools to characterize the size and size heterogeneity of large (above 15 nm) lipid nanoparticles encased by the diisobutylene/maleic acid (DIBMA) copolymer at different DIBMA/lipid ratios and percentages of anionic lipids. Importantly, for nanoparticle preparations in the diameter range of 40 nm or below, the size homogeneity of the DIBMA/lipid nanoparticles (DIBMALPs) remains unchanged. In addition, we show that anionic lipids do not affect the production, size and size homogeneity of DIBMALPs. Furthermore, they do not affect the overall lipid dynamics in the membrane, and preserve the functionality of an enclosed membrane protein. This work strengthens the suitability of DIBMALPs as universal, native-like lipid environments for functional studies of membrane proteins and provide useful insight on the suitability of these systems for those structural techniques requiring highly homogeneous sample preparations.
dc.description.sponsorshipGerman Research Foundation (DFG)German Research Foundation (DFG) [STE640/15, SFB 944/3 - 2020, SFB 944]; The authors thank John Danial for carefully reading the manuscript. This work was supported by German Research Foundation (DFG, STE640/15) to H.J.S, (DFG, SFB 944/3 - 2020, P 26) to K.C. and (DFG, SFB 944 Z-Project) to O.E.P. The TEM and AFM imaging was performed in the electron microscopy and optical imaging unit of Integrated Bioimaging Facility (iBiOs) at the Center of Cellular Nanoanalytics (CellNanOs), University of Osnabruck.
dc.language.isoen
dc.publisherELSEVIER
dc.relation.ispartofBIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
dc.subjectAmphiphilic maleic acid-containing polymers
dc.subjectAnionic lipids
dc.subjectBiochemistry & Molecular Biology
dc.subjectBiophysics
dc.subjectDIBMALPs
dc.subjectMembrane protein complexes
dc.subjectModel membranes
dc.titleEvaluation of DIBMA nanoparticles of variable size and anionic lipid content as tools for the structural and functional study of membrane proteins
dc.typejournal article
dc.identifier.doi10.1016/j.bbamem.2021.183588
dc.identifier.isiISI:000634801700004
dc.description.volume1863
dc.description.issue6
dc.contributor.orcid0000-0002-5888-0157
dc.contributor.orcid0000-0003-0571-3563
dc.contributor.orcid0000-0002-3796-3500
dc.contributor.researcheridH-3791-2014
dc.identifier.eissn18792642
dc.publisher.placeRADARWEG 29, 1043 NX AMSTERDAM, NETHERLANDS
dcterms.isPartOf.abbreviationBiochim. Biophys. Acta-Biomembr.
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptFB 04 - Physik-
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb04-
crisitem.author.deptidfb05-
crisitem.author.deptidfb04-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0003-2317-0144-
crisitem.author.orcid0000-0002-4035-6840-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidVoNa568-
crisitem.author.netidPsOl764-
crisitem.author.netidStHe633-
crisitem.author.netidCoKa893-
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