ArticleThe Journal of biological chemistry2017
Heparin-dependent aggregation of hen egg white lysozyme reveals two distinct mechanisms of amyloid fibrillation.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.Protein science : a publication of the Protein Society · 2025Article
- Article
- Nanocellulose aerogels as 3D amyloid templates.Nanoscale · 2023Article
- Roles of Tryptophan and Charged Residues on the Polymorphisms of Amyloids Formed by K-Peptides of Hen Egg White Lysozyme Investigated through Molecular Dynamics Simulations.International journal of molecular sciences · 2023Article
- Mechanisms of polyphosphate-induced amyloid fibril formation triggered by breakdown of supersaturation.Biophysics and physicobiology · 2023Article
- Controlling Amyloid Fibril Properties Via Ionic Liquids: The Representative Case of Ethylammonium Nitrate and Tetramethylguanidinium Acetate on the Amyloidogenesis of Lysozyme.The journal of physical chemistry letters · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Breakdown of supersaturation barrier links protein folding to amyloid formation.Communications biology · 2021Article
- Article
- A simple method for modeling amyloid kinetics featuring position biased fiber breakage.Biophysics and physicobiology · 2020Article
- Article
- Heating during agitation of βThe Journal of biological chemistry · 2019Article
- Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation.The Journal of biological chemistry · 2019Article
- Possible mechanisms of polyphosphate-induced amyloid fibril formation of βProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Aggregation-phase diagrams of βThe Journal of biological chemistry · 2018Article
- Salt-induced formations of partially folded intermediates and amyloid fibrils suggests a common underlying mechanism.Biophysical reviews · 2018Review
- Formation and properties of amyloid fibrils of prion protein.Biophysical reviews · 2018Review
- Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners.The Journal of biological chemistryArticle
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Authors and funding
11 authors at 7 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Heparin, a biopolymer possessing high negative charge density, is known to accelerate amyloid fibrillation by various proteins. Using hen egg white lysozyme, we studied the effects of heparin on protein aggregation at low pH, raised temperature, and applied ultrasonic irradiation, conditions under which amyloid fibrillation was promoted. Heparin exhibited complex bimodal concentration-dependent effects, either accelerating or inhibiting fibrillation at pH 2.0 and 60 °C. At concentrations lower than 20 μg/ml, heparin accelerated fibrillation through transient formation of hetero-oligomeric aggregates. Between 0.1 and 10 mg/ml, heparin rapidly induced amorphous heteroaggregation with little to no accompanying fibril formation. Above 10 mg/ml, heparin again induced fibrillation after a long lag time preceded by oligomeric aggregate formation. Compared with studies performed using monovalent and divalent anions, the results suggest two distinct mechanisms of heparin-induced fibrillation. At low heparin concentrations, initial hen egg white lysozyme cluster formation and subsequent fibrillation is promoted by counter ion binding and screening of repulsive charges. At high heparin concentrations, fibrillation is caused by a combination of salting out and macromolecular crowding effects probably independent of protein net charge. Both fibrillation mechanisms compete against amorphous aggregation, producing a complex heparin concentration-dependent phase diagram. Moreover, the results suggest an active role for amorphous oligomeric aggregates in triggering fibrillation, whereby breakdown of supersaturation takes place through heterogeneous nucleation of amyloid on amorphous aggregates.
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