ArticleProceedings of the National Academy of Sciences of the United States of America2012
Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 72 citations in OpenAlex.
- Proteolysis of apolipoprotein A-I by secretory phospholipase A₂: a new link between inflammation and atherosclerosis.The Journal of biological chemistry · 2014Trial
- Serum-tolerant polymeric complex for stem-cell transfection and neural differentiation.Nature communications · 2025Article
- Molecular Simulation of the Binding of Amyloid Beta to Apolipoprotein A-I in High-Density Lipoproteins.International journal of molecular sciences · 2025Article
- An atomistic characterization of high-density lipoproteins and the conserved "LN" region of apoA-I.Biophysical journal · 2024Article
- The role of C-terminal ionic residues in self-association of apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2023Article
- The HDL particle composition determines its antitumor activity in pancreatic cancer.Life science alliance · 2022Article
- Conformational flexibility of apolipoprotein A-I amino- and carboxy-termini is necessary for lipid binding but not cholesterol efflux.Journal of lipid research · 2022Article
- Fragments ofBBA advances · 2021Article
- rHDL modeling and the anchoring mechanism of LCAT activation.Journal of lipid research · 2021Article
- OX-HDL: A Starring Role in Cardiorenal Syndrome and the Effects of Heme Oxygenase-1 Intervention.Diagnostics (Basel, Switzerland) · 2020Review
- Reconfiguring Nature's Cholesterol Accepting Lipoproteins as Nanoparticle Platforms for Transport and Delivery of Therapeutic and Imaging Agents.Nanomaterials (Basel, Switzerland) · 2020Review
- Structural analysis of lecithin:cholesterol acyltransferase bound to high density lipoprotein particles.Communications biology · 2020Article
- Article
- The Extent of Human Apolipoprotein A-I Lipidation Strongly Affects the β-Amyloid Efflux Across the Blood-Brain BarrierFrontiers in neuroscience · 2019Article
- Molecular dynamics simulations of lipid nanodiscs.Biochimica et biophysica acta. Biomembranes · 2018Article
- Effects of Disease-Causing Mutations on the Conformation of Human Apolipoprotein A-I in Model Lipoproteins.Biochemistry · 2018Article
- Interaction of lecithin:cholesterol acyltransferase with lipid surfaces and apolipoprotein A-I-derived peptides.Journal of lipid research · 2018Article
- Arginine 123 of apolipoprotein A-I is essential for lecithin:cholesterol acyltransferase activity.Journal of lipid research · 2018Article
- Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity.Biochimica et biophysica acta. Biomembranes · 2017Article
- Immunochemical Approach for Monitoring of Structural Transition of ApoA-I upon HDL Formation Using Novel Monoclonal Antibodies.Scientific reports · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
To understand high-density lipoprotein (HDL) structure at the molecular level, the location and stability of α-helical segments in human apolipoprotein (apo) A-I in large (9.6 nm) and small (7.8 nm) discoidal HDL particles were determined by hydrogen-deuterium exchange (HX) and mass spectrometry methods. The measured HX kinetics of some 100 apoA-I peptides specify, at close to amino acid resolution, the structural condition of segments throughout the protein sequence and changes in structure and stability that occur on incorporation into lipoprotein particles. When incorporated into the large HDL particle, the nonhelical regions in lipid-free apoA-I (residues 45-53, 66-69, 116-146, and 179-236) change conformation from random coil to α-helix so that nearly the entire apoA-I molecule adopts helical structure (except for the terminal residues 1-6 and 237-243). The amphipathic α-helices have relatively low stability, in the range 3-5 kcal/mol, indicating high flexibility and dynamic unfolding and refolding in seconds or less. A segment encompassed by residues 125-158 exhibits bimodal HX labeling indicating co-existing helical and disordered loop conformations that interchange on a time scale of minutes. When incorporated around the edge of the smaller HDL particle, the increase in packing density of the two apoA-I molecules forces about 20% more residues out of direct contact with the phospholipid molecules to form disordered loops, and these are the same segments that form loops in the lipid-free state. The region of disc-associated apoA-I that binds the lecithin-cholesterol acyltransferase enzyme is well structured and not a protruding unstructured loop as reported by others.
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