ArticleProceedings of the National Academy of Sciences of the United States of America2006
Apolipoprotein B is conformationally flexible but anchored at a triolein/water interface: a possible model for lipoprotein surfaces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
- Article
- Non-alcoholic fatty liver disease in a pediatric patient with heterozygous familial hypobetalipoproteinemia due to a novelFrontiers in medicine · 2023Article
- A New Structural Model of Apolipoprotein B100 Based on Computational Modeling and Cross Linking.International journal of molecular sciences · 2022Article
- Identification of 121 variants of honey bee Vitellogenin protein sequences with structural differences at functional sites.Protein science : a publication of the Protein Society · 2022Article
- How Honey Bee Vitellogenin Holds Lipid Cargo: A Role for the C-Terminal.Frontiers in molecular biosciences · 2022Article
- High hydrostatic pressure specifically affects molecular dynamics and shape of low-density lipoprotein particles.Scientific reports · 2017Article
- A minimal length rigid helical peptide motif allows rational design of modular surfactants.Nature communications · 2017Article
- Apolipoprotein A-I mimetic peptide 4F blocks sphingomyelinase-induced LDL aggregation.Journal of lipid research · 2015Article
- Low-density lipoprotein-mediated delivery of docosahexaenoic acid selectively kills murine liver cancer cells.Nanomedicine (London, England) · 2014Article
- Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces.Journal of lipid research · 2014Article
- Human LDL structural diversity studied by IR spectroscopy.PloS one · 2014Article
- Interfacial properties of high-density lipoprotein-like lipid droplets with different lipid and apolipoprotein A-I compositions.Biophysical journal · 2013Article
- Lipids and HCV.Seminars in immunopathology · 2013Review
- Softness of atherogenic lipoproteins: a comparison of very low density lipoprotein (VLDL) and low density lipoprotein (LDL) using elastic incoherent neutron scattering (EINS).Journal of the American Chemical Society · 2011Article
- C-terminus of apolipoprotein A-I removes phospholipids from a triolein/phospholipids/water interface, but the N-terminus does not: a possible mechanism for nascent HDL assembly.Biophysical journal · 2011Article
- Immuno-electron cryo-microscopy imaging reveals a looped topology of apoB at the surface of human LDL.Journal of lipid research · 2011Article
- Three-dimensional cryoEM reconstruction of native LDL particles to 16Å resolution at physiological body temperature.PloS one · 2011Article
- Effects of phospholipase A(2) and its products on structural stability of human LDL: relevance to formation of LDL-derived lipid droplets.Journal of lipid research · 2011Article
- Apo B100 similarities to viral proteins suggest basis for LDL-DNA binding and transfection capacity.Journal of lipid research · 2010Article
- Interfacial properties of apolipoprotein B292-593 (B6.4-13) and B611-782 (B13-17). Insights into the structure of the lipovitellin homology region in apolipoprotein B.Biochemistry · 2010Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Apolipoprotein B (apoB) is one of a unique group of proteins that form and bind to fat droplets, stabilize the emulsified fat, and direct their metabolism. ApoB, secreted on lipoproteins (emulsions), remains bound during lipid metabolism yet exhibits conformational flexibility. It has amphipathic beta-strand (AbetaS)-rich domains and amphipathic alpha-helix (AalphaH)-rich domains. We showed that two consensus AbetaS peptides of apoB bound strongly to hydrophobic interfaces [triolein/water (TO/W) and dodecane/water], were elastic, and were not pushed off the interface when the surface was compressed. In contrast, an AalphaH peptide modeling helical parts of apoB was forced off the TO/W interface by compression and readsorbed when the interface was expanded. In this report, the surface behavior of apoB-100 was studied at the TO/W interface. Solubilized apoB lowered the interfacial tension of TO/W in a concentration-dependent fashion. At equilibrium tension, if the surface was compressed, part of apoB was pushed off but quickly readsorbed when the surface was expanded. Even when the surface area was compressed by approximately 55%, part of the apoB molecule remained bound. The maximum surface pressure that apoB could withstand without being partially ejected was 13 mN/m. ApoB showed high elasticity at the TO/W interface. Based on studies of the consensus AbetaS and AalphaH peptides, we suggest that AbetaSs anchor apoB and are its nonexchangeable motif, whereas its conformational flexibility arises from both the elastic nature of the AbetaS and the ability of AalphaH domains of the molecule to desorb and readsorb rapidly in response to surface pressure changes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.