ArticleProceedings of the National Academy of Sciences of the United States of America2007
Nucleation of protein fibrillation by nanoparticles.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 221 papers, 1 of them a synthesis that pooled it.
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Who cites it
221 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Systematic review of the osteogenic effect of rare earth nanomaterials and the underlying mechanisms.Journal of nanobiotechnology · 2024Pooled it
- Amino Acid-Driven Gold Nanochaperone Platforms for Alzheimer's Therapy: A Mechanistic and Design Framework for Protein Misfolding Modulation.Molecular neurobiology · 2026Review
- Does amyloid fibril nucleation occur at surfaces only?Biophysical journal · 2026Article
- Pollutants regulate changes in pathological markers of neurodegenerative diseases: a new perspective in environmental toxicology.Frontiers in toxicology · 2026Review
- On the background of plastics nanoparticles in our research.Frontiers in toxicology · 2026Article
- Nanosystems Containing Proteins: From Fundamentals to Applications.Chemistry, an Asian journal · 2026Review
- Structural and conformational rearrangements of human serum albumin, transferrin, and blood plasma induced by carbosilane dendrimer therapeutic delivery system.Scientific reports · 2025Article
- Physiological pH Transition-Driven Protein Corona Dynamics Regulate Cellular Uptake and Inflammatory Responses of Silica Nanoparticles.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Disease-disease interactions: molecular links of neurodegenerative diseases with cancer, viral infections, and type 2 diabetes.Translational neurodegeneration · 2025Review
- Aβ42 promotes the aggregation of α-synuclein splice isoforms via heterogeneous nucleation.FEBS letters · 2025Article
- Microglial Clearance of Alzheimer's Amyloid-Beta Obstructed by Nanoplastics.Environmental science. Nano · 2025Article
- The Effect of Polyethylene Terephthalate Nanoplastics on Amyloid-β Peptide Fibrillation.Molecules (Basel, Switzerland) · 2025Article
- Review
- The question of strains in AA amyloidosis.Scientific reports · 2025Article
- Helicobacter pylori outer membrane vesicles directly promote Aβ aggregation and enhance Aβ toxicity in APP/PS1 mice.Communications biology · 2024Article
- Polystyrene nanoparticles trigger aberrant condensation of TDP-43 and amyotrophic lateral sclerosis-like symptoms.Nature nanotechnology · 2024Article
- A comprehensive investigation of the interactions of human serum albumin with polymeric and hybrid nanoparticles.Drug delivery and translational research · 2024Article
- Nanoparticle-assisted tubulin assembly is environment dependent.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The role of shear forces in primary and secondary nucleation of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mechanistic Insights Behind the Self-Assembly of Human Insulin under the Influence of Surface-Engineered Gold Nanoparticles.ACS chemical neuroscience · 2024Article
161 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Nanoparticles present enormous surface areas and are found to enhance the rate of protein fibrillation by decreasing the lag time for nucleation. Protein fibrillation is involved in many human diseases, including Alzheimer's, Creutzfeld-Jacob disease, and dialysis-related amyloidosis. Fibril formation occurs by nucleation-dependent kinetics, wherein formation of a critical nucleus is the key rate-determining step, after which fibrillation proceeds rapidly. We show that nanoparticles (copolymer particles, cerium oxide particles, quantum dots, and carbon nanotubes) enhance the probability of appearance of a critical nucleus for nucleation of protein fibrils from human beta(2)-microglobulin. The observed shorter lag (nucleation) phase depends on the amount and nature of particle surface. There is an exchange of protein between solution and nanoparticle surface, and beta(2)-microglobulin forms multiple layers on the particle surface, providing a locally increased protein concentration promoting oligomer formation. This and the shortened lag phase suggest a mechanism involving surface-assisted nucleation that may increase the risk for toxic cluster and amyloid formation. It also opens the door to new routes for the controlled self-assembly of proteins and peptides into novel nanomaterials.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.