ArticleProceedings of the National Academy of Sciences of the United States of America2020
Physical mechanisms of amyloid nucleation on fluid membranes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 43 citations in OpenAlex.
- Article
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Effect of Tau Fragment and Membrane Interactions on Membrane Permeabilization and Peptide Aggregation.Membranes · 2025Article
- Amyloid beta (Aβ) fibrillation kinetics and its impact on membrane polarity.Journal of bioenergetics and biomembranes · 2025Article
- Pore Formation by Amyloid-like Peptides: Effects of the Nonpolar-Polar Sequence Pattern.ACS chemical neuroscience · 2024Article
- Self-replication of AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Ambient Temperature Affects Protein Self-Assembly by Interfering with the Interfacial Aggregation Behavior.ACS omega · 2023Article
- Lipid oxidation controls peptide self-assembly near membranes through a surface attraction mechanism.Chemical science · 2023Article
- A Nanoparticle-Based Model System for the Study of Heterogeneous Nucleation Phenomena.Langmuir : the ACS journal of surfaces and colloids · 2023Article
- Adsorption free energy predicts amyloid protein nucleation rates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Conformational entropy limits the transition from nucleation to elongation in amyloid aggregation.Biophysical journal · 2022Article
- The Small Heat Shock Protein, HSPB1, Interacts with and Modulates the Physical Structure of Membranes.International journal of molecular sciences · 2022Article
- Large self-assembled clathrin lattices spontaneously disassemble without sufficient adaptor proteins.PLoS computational biology · 2022Article
- Interaction of membrane vesicles with theBBA advances · 2022Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Pathway Complexity in Supramolecular Porphyrin Self-Assembly at an Immiscible Liquid-Liquid Interface.Journal of the American Chemical Society · 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
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Biological membranes can dramatically accelerate the aggregation of normally soluble protein molecules into amyloid fibrils and alter the fibril morphologies, yet the molecular mechanisms through which this accelerated nucleation takes place are not yet understood. Here, we develop a coarse-grained model to systematically explore the effect that the structural properties of the lipid membrane and the nature of protein-membrane interactions have on the nucleation rates of amyloid fibrils. We identify two physically distinct nucleation pathways-protein-rich and lipid-rich-and quantify how the membrane fluidity and protein-membrane affinity control the relative importance of those molecular pathways. We find that the membrane's susceptibility to reshaping and being incorporated into the fibrillar aggregates is a key determinant of its ability to promote protein aggregation. We then characterize the rates and the free-energy profile associated with this heterogeneous nucleation process, in which the surface itself participates in the aggregate structure. Finally, we compare quantitatively our data to experiments on membrane-catalyzed amyloid aggregation of α-synuclein, a protein implicated in Parkinson's disease that predominately nucleates on membranes. More generally, our results provide a framework for understanding macromolecular aggregation on lipid membranes in a broad biological and biotechnological context.
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