ArticleInternational journal of biological sciences2013
Analysis of core region from egg white lysozyme forming amyloid fibrils.
Article in International journal of biological sciences, 2013. 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, 82 citations in OpenAlex.
- Spirooxindoles as Disruptors of Preformed Hen Egg White Lysozyme Fibrils as a Model for Neurodegenerative Diseases.ChemMedChem · 2026Article
- Psoralen and Seselin Stabilize the α-helix Structure in Lysozyme and Inhibit the α-helix to β-sheet Exchange: An Efficient Anti-Amyloidogenic Mechanism.Advanced pharmaceutical bulletin · 2026Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- Inhibition of cytotoxic self-assembly of HEWL through promoting fibrillation by new synthesized α-hydroxycarbamoylphosphinic acids.RSC advances · 2024Article
- Mechanism of Reduced Glutathione Induced Lysozyme Defolding and Molecular Self-Assembly.Foods (Basel, Switzerland) · 2023Article
- Analysis of the enzymatic degradation of lysozyme fibrils using a combination method of non-denaturing gel electrophoresis and double staining with Coomassie Brilliant Blue G-250 and R-250 dyes.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 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
- A Diphenylalanine Based Pentapeptide with Fibrillating Self-Assembling Properties.Pharmaceutics · 2023Article
- Repression Effects of Hydrolysates from Hen-Egg Proteins on Amyloid Fibril Formation.The journal of poultry science · 2022Article
- One- and Two-Photon Excited Autofluorescence of Lysozyme Amyloids.The journal of physical chemistry letters · 2022Article
- Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation.International journal of molecular sciences · 2022Article
- DMSO and TMAO-Differences in Interactions in Aqueous Solutions of the K-Peptide.International journal of molecular sciences · 2022Article
- Article
- UV Resonance Raman explores protein structural modification upon fibrillation and ligand interaction.Biophysical journal · 2021Article
- Article
- Mechanisms for the inhibition of amyloid aggregation by small ligands.Bioscience reports · 2016Article
- Lysozyme Mutants Accumulate in Cells while Associated at their N-terminal Alpha-domain with the Endoplasmic Reticulum Chaperone GRP78/BiP.International journal of biological sciences · 2016Article
- Unraveling Comparative Anti-Amyloidogenic Behavior of Pyrazinamide and D-Cycloserine: A Mechanistic Biophysical Insight.PloS one · 2015Article
- Article
- Amyloid fibril formation in vitro from halophilic metal binding protein: its high solubility and reversibility minimized formation of amorphous protein aggregations.Protein science : a publication of the Protein Society · 2013Article
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Authors and funding
5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Some of the lysozyme mutants in humans cause systemic amyloidosis. Hen egg white lysozyme (HEWL) has been well studied as a model protein of amyloid fibrils formation. We previously identified an amyloid core region consisting of nine amino acids (designated as the K peptide), which is present at 54-62 in HEWL. The K peptide, with tryptophan at its C- terminus, has the ability of self-aggregation. In the present work we focused on its structural properties in relation to the formation of fibrils. The K peptide alone formed definite fibrils having β-sheet structures by incubation of 7 days under acidic conditions at 37°C. A substantial number of fibrils were generated under this pH condition and incubation period. Deletion and substitution of tryptophan in the K peptide resulted in no formation of fibrils. Tryptophan 62 in lysozyme was suggested to be especially crucial to forming amyloid fibrils. We also show that amyloid fibrils formation of the K peptide requires not only tryptophan 62 but also a certain length containing hydrophobic amino acids. A core region is involved in the significant formation of amyloid fibrils of lysozyme.
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