ArticleJournal of the American Chemical Society2009
Structures of beta-amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with gamma-secretase.
Article in Journal of the American Chemical Society, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
- Damage of the Phospholipid Bilayer by Aβ42 at Physiologically Relevant Peptide Concentrations.ACS chemical neuroscience · 2024Article
- Helix-to-sheet transition of the Aβ42 peptide revealed using an enhanced sampling strategy and Markov state model.Computational and structural biotechnology journal · 2024Article
- Silver nanoparticles alter the dimerization of AβRSC advances · 2024Article
- Current and further outlook on the protective potential ofFrontiers in pharmacology · 2024Review
- Imaging Amyloid-β Membrane Interactions: Ion-Channel Pores and Lipid-Bilayer Permeability in Alzheimer's Disease.Angewandte Chemie (International ed. in English) · 2023Review
- Imaging Amyloid-β Membrane Interactions: Ion-Channel Pores and Lipid-Bilayer Permeability in Alzheimer's Disease.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2023Review
- Formation of extramembraneProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Electrografting a Hybrid Bilayer Membrane via Diazonium Chemistry for Electrochemical Impedance Spectroscopy of Amyloid-β Aggregation.Micromachines · 2022Article
- Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The Role of Cholesterol in Amyloidogenic Substrate Binding to the γ-Secretase Complex.Biomolecules · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- EspcTM: Kinetic Transition Network Based on Trajectory Mapping in Effective Energy Rescaling Space.Frontiers in molecular biosciences · 2020Article
- Structure and Function of Alzheimer's Amyloid βeta Proteins from Monomer to Fibrils: A Mini Review.The protein journal · 2019Review
- Increased H-Bond Stability Relates to Altered ε-Cleavage Efficiency and Aβ Levels in the I45T Familial Alzheimer's Disease Mutant of APP.Scientific reports · 2019Article
- Structure of APP-C99Biochimica et biophysica acta. Biomembranes · 2018Article
- Similarity search combined with docking and molecular dynamics for novel hAChE inhibitor scaffolds.Journal of molecular modeling · 2018Article
- How accurate are your simulations? Effects of confined aqueous volume and AMBER FF99SB and CHARMM22/CMAP force field parameters on structural ensembles of intrinsically disordered proteins: Amyloid-βIntrinsically disordered proteins · 2017Article
- Interference of α-Synuclein Uptake by Monomeric β-Amyloid1-40 and Potential Core Acting Site of the Interference.Neurotoxicity research · 2016Article
- Impact of membrane lipid composition on the structure and stability of the transmembrane domain of amyloid precursor protein.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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3 authors.
Funding
Abstract
Aggregation of Amyloid beta (Abeta) peptide has been linked to the neurodegenerative Alzheimer's Disease and implicated in other amyloid diseases including cerebral amyloid angiopathy. Abeta peptide is generated by cleavage of the amyloid precursor protein (APP) by transmembrane proteases. It is crucial to determine the structures of beta-amyloid peptides in a membrane to provide a molecular basis for the cleavage mechanism. We report the structures of amyloid beta peptide (Abeta(1-40) and Abeta(1-42)) as well as the 672-726 fragment of APP (referred to as Abeta(1-55)) in a membrane environment determined by replica-exchange molecular dynamics simulation. Abeta(1-40) is found to have two helical domains A (13-22) and B(30-35) and a type I beta-turn at 23-27. The peptide is localized at the interface between membrane and solvent. Substantial fluctuations in domain A are observed. The dominant simulated tertiary structure of Abeta(1-40) is observed to be similar to the simulated Abeta(1-42) structure. However, there are differences observed in the overall conformational ensemble, as characterized by the two-dimensional free energy surfaces. The fragment of APP (Abeta(1-55)) is observed to have a long transmembrane helix. The position of the transmembrane region and ensemble of membrane structures are elucidated. The conformational transition between the transmembrane Abeta(1-55) structure, prior to cleavage, and the Abeta(1-40) structure, following cleavage, is proposed.
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