ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2015
Lysozyme stability and amyloid fibrillization dependence on Hofmeister anions in acidic pH.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 35 citations in OpenAlex.
- Protein Nanofibrils as Emerging Biomaterials for Sustainable Food Packaging: Advances, Challenges, and Future Opportunities.Comprehensive reviews in food science and food safety · 2026Review
- Role of Anion Identity in the Assembly and Morphology of Whey Protein Isolate Nanofibril Aggregates.Foods (Basel, Switzerland) · 2026Article
- Anion-Facilitated Hydrogen-Deuterium Exchange as a Tool to Probe Weak Anion-Protein Interactions Responsible for Hofmeister Effects.The journal of physical chemistry. B · 2025Article
- Anion Binding to Ammonium and Guanidinium Hosts: Implications for the Reverse Hofmeister Effects Induced by Lysine and Arginine Residues.The Journal of organic chemistry · 2024Article
- Assessing Weak Anion Binding to Small Peptides.The journal of physical chemistry. B · 2024Article
- Only kosmotrope anions trigger fibrillization of the recombinant core spidroin eADF4(C16) from Araneus diadematus.Protein science : a publication of the Protein Society · 2023Article
- Modulation of Insulin Amyloid Fibrillization in Imidazolium-Based Ionic Liquids with Hofmeister Series Anions.International journal of molecular sciences · 2023Article
- The influence of cations on α-lactalbumin amyloid aggregation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Article
- Differences in interaction lead to the formation of different types of insulin amyloid.Scientific reports · 2022Article
- Taurine Stabilizing Effect on Lysozyme.Life (Basel, Switzerland) · 2022Article
- Effect of 1-Ethyl-3-methylimidazolium Tetrafluoroborate and Acetate Ionic Liquids on Stability and Amyloid Aggregation of Lysozyme.International journal of molecular sciences · 2022Article
- Trehalose Effect on the Aggregation of Model Proteins into Amyloid Fibrils.Life (Basel, Switzerland) · 2020Article
- The Role of Buffers in Wild-Type HEWL Amyloid Fibril Formation Mechanism.Biomolecules · 2019Article
- Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Biophysical journal · 2017Article
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8 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
We have explored an effect of Hofmeister anions, Na2SO4, NaCl, NaBr, NaNO3, NaSCN and NaClO4, on stability and amyloid fibrillization of hen egg white lysozyme at pH 2.7. The stability of the protein was analyzed by differential scanning calorimetry. The Hofmeister effect of the anions was assessed by the parameter dT trs/d[anion] (T trs, transition temperature). We show that dT trs/d[anion] correlates with anion surface tension effects and anion partition coefficients indicating direct interactions between anions and lysozyme. The kinetic of amyloid fibrillization of lysozyme was followed by Thioflavin T (ThT) fluorescence. Negative correlation between dT trs/d[anion] and the nucleation rate of fibrillization in the presence of monovalent anions indicates specific effect of anions on fibrillization rate of lysozyme. The efficiency of monovalent anions to accelerate fibrillization correlates with inverse Hofmeister series. The far-UV circular dichroism spectroscopy and atomic force microscopy findings show that conformational properties of fibrils depend on fibrillization rate. In the presence of sodium chloride, lysozyme forms typical fibrils with elongated structure and with the secondary structure of the β-sheet. On the other hand, in the presence of both chaotropic perchlorate and kosmotropic sulfate anions, the fibrils form clusters with secondary structure of β-turn. Moreover, the acceleration of fibril formation is accompanied by decreased amount of the formed fibrils as indicated by ThT fluorescence. Taken together, our study shows Hofmeister effect of monovalent anions on: (1) lysozyme stability; (2) ability to accelerate nucleation phase of lysozyme fibrillization; (3) amount, and (4) conformational properties of the formed fibrils.
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