ArticleProtein science : a publication of the Protein Society2013
Mechanism for retardation of amyloid fibril formation by sugars in Vλ6 protein.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- FreePlant biotechnology (Tokyo, Japan) · 2025Article
- The inhibition of fibril formation of lysozyme by sucrose and trehalose.RSC advances · 2024Article
- Understanding the impact of mannitol on physical stability and aerosolization of spray-dried protein powders for inhalation.International journal of pharmaceutics · 2024Article
- Trehalose-Bearing Carriers to Target Impaired Autophagy and Protein Aggregation Diseases.Journal of medicinal chemistry · 2023Review
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Investigating the stabilisation of IFN-α2a by replica exchange molecular dynamics simulation.Journal of molecular modeling · 2022Article
- Protein Fibrillation under Crowded Conditions.Biomolecules · 2022Review
- Effect of buffer additives on solubilization and refolding of reteplase inclusion bodies.Research in pharmaceutical sciences · 2018Article
- Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.The Journal of biological chemistry · 2017Article
- Denatured mammalian protein mixtures exhibit unusually high solubility in nucleic acid-free pure water.PloS one · 2014Article
- Mechanistic investigation of domain specific unfolding of human serum albumin and the effect of sucrose.Protein science : a publication of the Protein Society · 2013Article
- Protein folding and aggregation into amyloid: the interference by natural phenolic compounds.International journal of molecular sciences · 2013Review
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7 authors.
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Abstract
Sugars, which function as osmolytes within cells, retard the amyloid fibril formation of the amyloidosis peptides and proteins. To examine the mechanism of this retardation in detail, we analyzed the effect of sugars (trehalose, sucrose, and glucose) on the polypeptide chains in 3Hmut Wil, which is formed by the mutation of three His residues in Wil mutant as a cause of amyloid light-chain (AL) amyloidosis, at pH 2, a pH condition under which 3Hmut Wil was almost denatured. Sugars caused the folding of 3Hmut Wil so that its polypeptide chains adopted a native-like rather than a denatured conformation, as suggested by tryptophan fluorescence, CD spectroscopy, and heteronuclear NMR. Furthermore, these sugars promoted the folding to a native-like conformation according to the effect of preferential hydration rather than direct interaction. However, the type of sugar had no effect on the elongation of amyloid fibrils. Therefore, it was concluded that sugar affected the thermodynamic stability of 3Hmut Wil but not the elongation of amyloid fibrils.
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