ArticleThe Journal of biological chemistry2012
Intra-membrane oligomerization and extra-membrane oligomerization of amyloid-β peptide are competing processes as a result of distinct patterns of motif interplay.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 43 citations in OpenAlex.
- Anionic Lipid Catalyzes the Generation of Cytotoxic Insulin Oligomers.Biomolecules · 2025Article
- Molecular insights into the primary nucleation of polymorphic amyloid β dimers in DOPC lipid bilayer membrane.Protein science : a publication of the Protein Society · 2022Article
- Endocytosis Is a Key Mode of Interaction between Extracellular β-Amyloid and the Cell Membrane.Biophysical journal · 2020Article
- Endosomal pH favors shedding of membrane-inserted amyloid-β peptide.Protein science : a publication of the Protein Society · 2019Article
- Impact of GMBiophysical journal · 2017Review
- Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- An Intrinsically Disordered Motif Mediates Diverse Actions of Monomeric C-reactive Protein.The Journal of biological chemistry · 2016Article
- Lipid insertion domain unfolding regulates protein orientational transition behavior in a lipid bilayer.Biophysical chemistry · 2015Article
- Soluble amyloid-β oligomers as synaptotoxins leading to cognitive impairment in Alzheimer's disease.Frontiers in cellular neuroscience · 2015Review
- Combined treatment with a BACE inhibitor and anti-Aβ antibody gantenerumab enhances amyloid reduction in APPLondon mice.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Structural evolution and membrane interactions of Alzheimer's amyloid-beta peptide oligomers: new knowledge from single-molecule fluorescence studies.Protein science : a publication of the Protein Society · 2014Review
- Single-molecule imaging reveals aβ42:aβ40 ratio-dependent oligomer growth on neuronal processes.Biophysical journal · 2013Article
- Thermodynamically stable amyloid-β monomers have much lower membrane affinity than the small oligomers.Frontiers in physiology · 2013Article
- Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.Biochemistry · 2012Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble oligomers of amyloid-β peptide (Aβ) are emerging as the primary neurotoxic species in Alzheimer disease, however, whether the membrane is among their direct targets that mediate the downstream adverse effects remains elusive. Herein, we show that multiple soluble oligomeric Aβ preparations, including Aβ-derived diffusible ligand, protofibril, and zinc-induced Aβ oligomer, exhibit much weaker capability to insert into the membrane than Aβ monomer. Aβ monomers prefer incorporating into membrane rather than oligomerizing in solution, and such preference can be reversed by the aggregation-boosting factor, zinc ion. Further analyses indicate that the membrane-embedded oligomers of Aβ are derived from rapid assembly of inserted monomers but not due to the insertion of soluble Aβ oligomers. By comparing the behavior of a panel of Aβ truncation variants, we demonstrate that the intra- and extra-membrane oligomerization are mutually exclusive processes that proceed through distinct motif interplay, both of which require the action of amino acids 37-40/42 to overcome the auto-inhibitory interaction between amino acids 29-36 and the N-terminal portion albeit via different mechanisms. These results indicate that intra- and extra-membrane oligomerization of Aβ are competing processes and emphasize a critical regulation of membrane on the behavior of Aβ monomer and soluble oligomers, which may determine distinct neurotoxic mechanisms.
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Registered trials
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