ArticleBiophysical journal2009
Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition.
Article in Biophysical journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Carbon nanotubes as neuroprotective agents.Exploration of neuroprotective therapy · 2024Article
- Nanotechnology-based Drug Delivery for Alzheimer's and Parkinson's Diseases.Current drug delivery · 2024Review
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Article
- Dynamics of Amyloid Formation from Simplified Representation to Atomistic Simulations.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Computer Simulations Aimed at Exploring Protein Aggregation and Dissociation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The Interplay between Whey Protein Fibrils with Carbon Nanotubes or Carbon Nano-Onions.Materials (Basel, Switzerland) · 2021Article
- The membrane axis of Alzheimer's nanomedicine.Advanced nanobiomed research · 2021Article
- Morphological Determinants of Carbon Nanomaterial-Induced Amyloid Peptide Self-Assembly.Frontiers in chemistry · 2020Article
- Destabilization of amyloid fibrils on interaction with MoSRSC advances · 2019Article
- Exploring the Mechanism of Inhibition of Au Nanoparticles on the Aggregation of Amyloid-β(16-22) Peptides at the Atom Level by All-Atom Molecular Dynamics.International journal of molecular sciences · 2018Article
- Stereochemistry and amyloid inhibition: Asymmetric triplex metallohelices enantioselectively bind to Aβ peptide.Science advances · 2018Article
- Modulating protein amyloid aggregation with nanomaterials.Environmental science. Nano · 2017Article
- Exploring Protein-Nanoparticle Interactions with Coarse-Grained Protein Folding Models.Small (Weinheim an der Bergstrasse, Germany) · 2017Article
- Effects of hydroxylated carbon nanotubes on the aggregation of Aβ16-22 peptides: a combined simulation and experimental study.Biophysical journal · 2014Article
- Chemical basis of interactions between engineered nanoparticles and biological systems.Chemical reviews · 2014Review
- Effects of Zn2+ binding on the structural and dynamic properties of amyloid β peptide associated with Alzheimer's disease: Asp1 or Glu11?ACS chemical neuroscience · 2013Article
- Molecular dynamics simulation studies of the structural response of an isolated Aβ1-42 monomer localized in the vicinity of the hydrophilic TiO 2 surface.European biophysics journal : EBJ · 2013Article
- Dimensionality of carbon nanomaterials determines the binding and dynamics of amyloidogenic peptides: multiscale theoretical simulations.PLoS computational biology · 2013Article
- Biochemistry of amyloid β-protein and amyloid deposits in Alzheimer disease.Cold Spring Harbor perspectives in medicine · 2012Review
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4 authors.
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Abstract
Recent experimental studies show that carbon nanotubes impact the aggregation process of proteins associated with neurodegenerative diseases. However, the details of molecular interactions between proteins and carbon nanotubes are still not well understood. In this study, we investigate the initial adsorption features and dynamics of the Alzheimer's amyloid-beta peptide spanning residues 25-35 (Abeta25-35) on a single-walled carbon nanotube (SWNT) surface using fully atomic molecular dynamics simulations (MD) in explicit solvent. The initial configurations of the Abeta25-35 peptides consist of two preformed bilayer beta-sheets, each with four or five beta-strands in parallel or mixed antiparallel-parallel orientations. Our simulations show, for what we believe is the first time, that two disjointed Abeta25-35 beta-sheets with mixed antiparallel-parallel strands can assemble into beta-barrels wrapping the SWNT. In contrast, both simulations of Abeta25-35 without SWNT, and simulations of SWNT-Abeta25-35 with purely parallel beta-strands, lead to disordered aggregates. We find that Abeta25-35 beta-barrel formation involves at least two steps: i), curving of the Abeta25-35 beta-sheets as a result of strong hydrophobic interactions with carbon nanotube concomitantly with dehydration of the SWNT-peptide interface; and ii), intersheet backbone hydrogen bond formation with fluctuating intrasheet hydrogen bonds. Detailed analysis of the conversion shows that beta-barrel formation on SWNT surface results from the interplay of dehydration and peptide-SWNT/peptide-peptide interactions. Implications of our results on amyloid fibril inhibition are discussed.
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