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

Autor(en): Voskoboynikova, Natalia 
Orekhov, Philipp
Bozdaganyan, Marine
Kodde, Felix
Rademacher, Malte
Schowe, Maurice
Budke-Gieseking, Annette
Brickwedde, Britta
Psathaki, Olympia-Ekaterini 
Mulkidjanian, Armen Y.
Cosentino, Katia 
Shaitan, Konstantin V. 
Steinhoff, Heinz-Juergen 
Stichwörter: BILAYER PROPERTIES; Biochemistry & Molecular Biology; CHARGED PHOSPHOLIPIDS; Chemistry; Chemistry, Multidisciplinary; coarse-grained (CG); electron paramagnetic resonance spectroscopy (EPR; ESR); FREE PURIFICATION; HELIX F; lipid nanodiscs; membrane protein; MEMBRANE-PROTEINS; molecular dynamics (MD); NATRONOBACTERIUM-PHARAONIS; NATRONOMONAS-PHARAONIS; negative-stain and cryo-transmission electron microscopy (EM); nitroxide spin label; phospholipid bilayer; polymer; SPIN-LABEL; TRANSDUCER PROTEIN HTRII; VERSATILE TOOL
Erscheinungsdatum: 2021
Herausgeber: MDPI
Journal: INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volumen: 22
Ausgabe: 5
Zusammenfassung: 
Amphiphilic 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.
DOI: 10.3390/ijms22052548

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