ArticleBiophysical journal2021
Zinc determines dynamical properties and aggregation kinetics of human insulin.
Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 23 citations in OpenAlex.
- Intermetallic nanoassemblies potentiate systemic STING activation.Science (New York, N.Y.) · 2026Article
- Anthraquinones Inhibit Insulin Amyloidosis in Crowded Environments.Molecules (Basel, Switzerland) · 2026Article
- Physicochemical Stability of Insulin and Analogues in Saline Infusion: Screening for Amyloid and Amorphous High-Molecular-Weight Material.ACS omega · 2026Article
- Interactions of Sucrose and Trehalose with Lysozyme in Different Media: A Perspective from Atomistic Molecular Dynamics Simulations.Molecular pharmaceutics · 2025Article
- Detection of insulin oligomeric forms by a novel surface plasmon resonance-diffusion coefficient based approach.Protein science : a publication of the Protein Society · 2024Article
- Carbon dots as a versatile tool to monitor insulin aggregation.Analytical and bioanalytical chemistry · 2023Article
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Authors and funding
11 authors at 8 institutions in 5 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein aggregation is a widespread process leading to deleterious consequences in the organism, with amyloid aggregates being important not only in biology but also for drug design and biomaterial production. Insulin is a protein largely used in diabetes treatment, and its amyloid aggregation is at the basis of the so-called insulin-derived amyloidosis. Here, we uncover the major role of zinc in both insulin dynamics and aggregation kinetics at low pH, in which the formation of different amyloid superstructures (fibrils and spherulites) can be thermally induced. Amyloid aggregation is accompanied by zinc release and the suppression of water-sustained insulin dynamics, as shown by particle-induced x-ray emission and x-ray absorption spectroscopy and by neutron spectroscopy, respectively. Our study shows that zinc binding stabilizes the native form of insulin by facilitating hydration of this hydrophobic protein and suggests that introducing new binding sites for zinc can improve insulin stability and tune its aggregation propensity.
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