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Quantifying size distributions of nanolipoprotein particles with single-particle analysis and molecular dynamic simulations
- Source :
- Journal of Lipid Research, Vol 49, Iss 7, Pp 1420-1430 (2008)
- Publication Year :
- 2008
-
Abstract
- Self-assembly of purified apolipoproteins and phospholipids results in the formation of nanometer-sized lipoprotein complexes, referred to as nanolipoprotein particles (NLPs). These bilayer constructs are fully soluble in aqueous environments and hold great promise as a model system to aid in solubilizing membrane proteins. Size variability in the self-assembly process has been recognized for some time, yet limited studies have been conducted to examine this phenomenon. Understanding the source of this heterogeneity may lead to methods to mitigate heterogeneity or to control NLP size, which may be important for tailoring NLPs for specific membrane proteins. Here, we have used atomic force microscopy, ion mobility spectrometry, and transmission electron microscopy to quantify NLP size distributions on the single-particle scale, specifically focusing on assemblies with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and a recombinant apolipoprotein E variant containing the N-terminal 22 kDa fragment (E422k). Four discrete sizes of E422k/DMPC NLPs were identified by all three techniques, with diameters centered at approximately 14.5, 19, 23.5, and 28 nm. Computer simulations suggest that these sizes are related to the structure and number of E422k lipoproteins surrounding the NLPs and particles with an odd number of lipoproteins are consistent with the double-belt model, in which at least one lipoprotein adopts a hairpin structure.
- Subjects :
- Models, Molecular
Protein Folding
Ion-mobility spectrometry
Lipoproteins
Single particle analysis
QD415-436
Microscopy, Atomic Force
Biochemistry
Molecular dynamics
Endocrinology
Microscopy, Electron, Transmission
ion mobility spectrometry
Microscopy
nanodiscs
atomic force microscopy
Atomic force microscopy
Chemistry
Bilayer
Computational Biology
Cell Biology
Protein Structure, Tertiary
Crystallography
Membrane protein
Transmission electron microscopy
Biophysics
Nanoparticles
lipids (amino acids, peptides, and proteins)
Electrophoresis, Polyacrylamide Gel
high density lipoproteins
Dimyristoylphosphatidylcholine
apolipoproteins
Subjects
Details
- ISSN :
- 00222275
- Volume :
- 49
- Issue :
- 7
- Database :
- OpenAIRE
- Journal :
- Journal of lipid research
- Accession number :
- edsair.doi.dedup.....ad828e6eeb44a33ef61b8c96ca1b4cb1