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Lipid Dynamics in Diisobutylene-Maleic Acid (DIBMA) Lipid Particles in Presence of Sensory Rhodopsin II

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https://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-202106105043
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dc.creatorVoskoboynikova, Natalia-
dc.creatorOrekhov, Philipp-
dc.creatorBozdaganyan, Marine-
dc.creatorKodde, Felix-
dc.creatorRademacher, Malte-
dc.creatorSchowe, Maurice-
dc.creatorBudke-Gieseking, Annette-
dc.creatorBrickwedde, Britta-
dc.creatorPsathaki, Olympia-Ekaterini-
dc.creatorMulkidjanian, Armen Y.-
dc.creatorCosentino, Katia-
dc.creatorShaitan, Konstantin V.-
dc.creatorSteinhoff, Heinz-Jürgen-
dc.date.accessioned2021-06-10T11:59:21Z-
dc.date.available2021-06-10T11:59:21Z-
dc.date.issued2021-03-04-
dc.identifier.citationVoskoboynikova N, Orekhov P, Bozdaganyan M, Kodde F, Rademacher M, Schowe M, Budke-Gieseking A, Brickwedde B, Psathaki O-E, Mulkidjanian AY, Cosentino K, Shaitan KV, Steinhoff H-J.: Lipid Dynamics in Diisobutylene-Maleic Acid (DIBMA) Lipid Particles in Presence of Sensory Rhodopsin II. International Journal of Molecular Sciences. 2021; 22(5):2548.ger
dc.identifier.urihttps://osnadocs.ub.uni-osnabrueck.de/handle/urn:nbn:de:gbv:700-202106105043-
dc.description.abstractAmphiphilic diisobutylene/maleic acid (DIBMA) copolymers extract lipid-encased membrane proteins from lipid bilayers in a detergent-free manner, yielding nanosized, discoidal DIBMA lipid particles (DIBMALPs). Depending on the DIBMA/lipid ratio, the size of DIBMALPs can be broadly varied which makes them suitable for the incorporation of proteins of different sizes. Here, we examine the influence of the DIBMALP sizes and the presence of protein on the dynamics of encased lipids. As shown by a set of biophysical methods, the stability of DIBMALPs remains unaffected at different DIBMA/lipid ratios. Coarse-grained molecular dynamics simulations confirm the formation of viable DIBMALPs with an overall size of up to 35 nm. Electron paramagnetic resonance spectroscopy of nitroxides located at the 5th, 12th or 16th carbon atom positions in phosphatidylcholine-based spin labels reveals that the dynamics of enclosed lipids are not altered by the DIBMALP size. The presence of the membrane protein sensory rhodopsin II from Natronomonas pharaonis (NpSRII) results in a slight increase in the lipid dynamics compared to empty DIBMALPs. The light-induced photocycle shows full functionality of DIBMALPs-embedded NpSRII and a significant effect of the protein-to-lipid ratio during preparation on the NpSRII dynamics. This study indicates a possible expansion of the applicability of the DIBMALP technology on studies of membrane protein–protein interaction and oligomerization in a constraining environment.eng
dc.relationhttps://doi.org/10.3390/ijms22052548ger
dc.rightsAttribution 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectnitroxide spin labeleng
dc.subjectelectron paramagnetic resonance spectroscopy (EPR; ESR)eng
dc.subjectpolymer/lipid nanodiscseng
dc.subjectphospholipid bilayereng
dc.subjectmembrane proteineng
dc.subjectnegative-stain and cryo-transmission electron microscopy (EM)eng
dc.subjectcoarse-grained (CG)eng
dc.subjectmolecular dynamics (MD)eng
dc.subject.ddc530 - Physikger
dc.titleLipid Dynamics in Diisobutylene-Maleic Acid (DIBMA) Lipid Particles in Presence of Sensory Rhodopsin IIeng
dc.typeEinzelbeitrag in einer wissenschaftlichen Zeitschrift [article]ger
orcid.creatorhttps://orcid.org/0000-0002-5137-303X-
orcid.creatorhttps://orcid.org/0000-0002-5888-0157-
orcid.creatorhttps://orcid.org/0000-0003-2317-0144-
orcid.creatorhttps://orcid.org/0000-0003-4078-4762-
dc.identifier.doi10.3390/ijms22052548-
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