ArticlePloS one2015
pH-Driven Polymorphism of Insulin Amyloid-Like Fibrils.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 69 citations in OpenAlex.
- Beyond Amyloids: Neuroprotective Potential of Betanin and its Derivatives Against Alpha-Synuclein Aggregates and ROS Overload in Parkinson's Disease.Journal of molecular neuroscience : MN · 2026Article
- Study of Insulin Aggregation and Fibril Structure under Different Environmental Conditions.International journal of molecular sciences · 2024Article
- Investigating lysozyme amyloid fibril formation and structural variability dependence on its initial folding state under different pH conditions.Protein science : a publication of the Protein Society · 2024Article
- Modulation of the Fibrillation Kinetics and Morphology of a Therapeutic Peptide by Cucurbit[7]uril.Molecular pharmaceutics · 2023Article
- Lysozyme Amyloid Fibril Structural Variability Dependence on Initial Protein Folding State.International journal of molecular sciences · 2022Article
- The intriguing dose-dependent effect of selected amphiphilic compounds on insulin amyloid aggregation: Focus on a cholesterol-based detergent, Chobimalt.Frontiers in molecular biosciences · 2022Article
- Article
- Coupling chemical biology and vibrational spectroscopy for studies of amyloids in vitro and in cells.Current opinion in chemical biology · 2021Review
- Aggregation Condition-Structure Relationship of Mouse Prion Protein Fibrils.International journal of molecular sciences · 2021Article
- Temperature-Dependent Structural Variability of Prion Protein Amyloid Fibrils.International journal of molecular sciences · 2021Article
- Lysozyme Fibrils Alter the Mechanism of Insulin Amyloid Aggregation.International journal of molecular sciences · 2021Article
- Interplay between epigallocatechin-3-gallate and ionic strength during amyloid aggregation.PeerJ · 2021Article
- Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains.Frontiers in molecular biosciences · 2021Review
- Exploring the occurrence of thioflavin-T-positive insulin amyloid aggregation intermediates.PeerJ · 2021Article
- Identifying Insulin Fibril Conformational Differences by Thioflavin-T Binding Characteristics.Biomacromolecules · 2020Article
- New Model for Stacking Monomers in Filamentous Actin from Skeletal Muscles ofInternational journal of molecular sciences · 2020Article
- Hydroxytyrosol Inhibits Protein Oligomerization and Amyloid Aggregation in Human Insulin.International journal of molecular sciences · 2020Article
- Formation of distinct prion protein amyloid fibrils under identical experimental conditions.Scientific reports · 2020Article
- Article
- Cross-Species and Cross-Polymorph Seeding of Lysozyme Amyloid Reveals a Dominant Polymorph.Frontiers in molecular biosciences · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are infective proteins, which can self-assemble into different strain conformations, leading to different disease phenotypes. An increasing number of studies suggest that prion-like self-propagation may be a common feature of amyloid-like structures. Thus it is important to unravel every possible factor leading to the formation of different amyloid strains. Here we report on the formation of two types of insulin amyloid-like fibrils with distinct infrared spectroscopic features grown under slightly different pH conditions. Similar to prion strains, both insulin fibril types are able to self-propagate their conformational template under conditions, favoring spontaneous formation of different type fibrils. The low-pH-induced insulin amyloid strain is structurally very similar to previously reported strains formed either in the presence of 20% ethanol, or by modification of the amino acid sequence of insulin. A deeper analysis of literature data in the context of our current findings suggests a shift of the monomer-dimer equilibrium of insulin as a possible factor controlling the formation of different strains.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.