ArticleScientific reports2017
Nano-assembly of amyloid β peptide: role of the hairpin fold.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Molecular Dynamics Simulations of AβACS omega · 2026Article
- A lattice Monte Carlo model for amyloid fibril formation.Biophysics and physicobiology · 2026Article
- The role of hydrophobic collapse in cytotoxic and functional amyloid oligomerization.Biophysical journal · 2025Article
- Sequence-based identification of amyloidogenic β-hairpins reveals a prostatic acid phosphatase fragment promoting semen amyloid formation.Computational and structural biotechnology journal · 2024Article
- Generative β-hairpin design using a residue-based physicochemical property landscape.Biophysical journal · 2024Article
- Why Is Arginine the Only Amino Acid That Inhibits Polyglutamine Monomers from Taking on Toxic Conformations?ACS chemical neuroscience · 2024Article
- Exploring Structural Insights of Aβ42 and α-Synuclein Monomers and Heterodimer: A Comparative Study Using Implicit and Explicit Solvent Simulations.The journal of physical chemistry. B · 2024Article
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Can local heating and molecular crowders disintegrate amyloid aggregates?Chemical science · 2024Article
- β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides.Biochemistry · 2024Article
- Nucleation of α-Synuclein Amyloid Fibrils Induced by Cross-Interaction with β-Hairpin Peptides Derived from Immunoglobulin Light Chains.International journal of molecular sciences · 2023Article
- Assembly of Synaptic Protein-DNA Complexes: Critical Role of Non-Specific Interactions.International journal of molecular sciences · 2023Article
- Key Residue for Aggregation of Amyloid-β Peptides.ACS chemical neuroscience · 2022Article
- Molecular Dynamics Simulation Studies on the Aggregation of Amyloid-β Peptides and Their Disaggregation by Ultrasonic Wave and Infrared Laser Irradiation.Molecules (Basel, Switzerland) · 2022Review
- Molecular dynamics simulations of amyloid-β peptides in heterogeneous environments.Biophysics and physicobiology · 2022Article
- Toxicity of internalized polyalanine to cells depends on aggregation.Scientific reports · 2021Article
- Promotion and Inhibition of Amyloid-β Peptide Aggregation: Molecular Dynamics Studies.International journal of molecular sciences · 2021Review
- AFM Probing of Amyloid-Beta 42 Dimers and Trimers.Frontiers in molecular biosciences · 2020Article
- Force clamp approach for characterization of nano-assembly in amyloid beta 42 dimer.Nanoscale · 2019Article
- Probing Intermolecular Interactions within the Amyloid β Trimer Using a Tethered Polymer Nanoarray.Bioconjugate chemistry · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Structural investigations have revealed that β hairpin structures are common features in amyloid fibrils, suggesting that these motifs play an important role in amyloid assembly. To test this hypothesis, we characterized the effect of the hairpin fold on the aggregation process using a model β hairpin structure, consisting of two Aβ(14-23) monomers connected by a turn forming YNGK peptide. AFM studies of the assembled aggregates revealed that the hairpin forms spherical structures whereas linear Aβ(14-23) monomers form fibrils. Additionally, an equimolar mixture of the monomer and the hairpin assembles into non-fibrillar aggregates, demonstrating that the hairpin fold dramatically changes the morphology of assembled amyloid aggregates. To understand the molecular mechanism underlying the role of the hairpin fold on amyloid assembly, we performed single-molecule probing experiments to measure interactions between hairpin and monomer and two hairpin complexes. The studies reveal that the stability of hairpin-monomer complexes is much higher than hairpin-hairpin complexes. Molecular dynamics simulations revealed a novel intercalated complex for the hairpin and monomer and Monte Carlo modeling further demonstrated that such nano-assemblies have elevated stability compared with stability of the dimer formed by Aβ(14-23) hairpin. The role of such folding on the amyloid assembly is also discussed.
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