ArticleMolecules (Basel, Switzerland)2022
Zinc and Copper Ions Induce Aggregation of Human β-Crystallins.
Article in Molecules (Basel, Switzerland), 2022. 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, 15 citations in OpenAlex.
- Size-shrinking nanoparticles with high drug-protein payload for efficient, non-invasive treatment of corneal neovascularization.Journal of nanobiotechnology · 2026Article
- Metal-Dependent Effects and Crowding Robustness of Pseudomonas fluorescens Esterase I.Chembiochem : a European journal of chemical biology · 2026Article
- Metal ions in aging and ocular diseases: biology, pathophysiology, and therapeutic strategies.npj aging · 2026Review
- Mini-αA-crystallin protects a client lens protein from catastrophic aggregation due to heat stress.Protein science : a publication of the Protein Society · 2025Article
- The interaction of Cu(II) and Zn(II) with peptide fragment of HSPB1 and its analogs.Frontiers in molecular biosciences · 2025Article
- Characterization of the Interaction of Human γS Crystallin with Metal Ions and Its Effect on Protein Aggregation.Biomolecules · 2024Article
- Review
- Glycyl-l-histidyl-l-lysine prevents copper- and zinc-induced protein aggregation and central nervous system cell death in vitro.Metallomics : integrated biometal science · 2024Article
- A bibliometric and visualized analysis of the pathogenesis of cataracts from 1999 to 2023.Heliyon · 2024Article
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- Selenium intake help prevent age-related cataract formation: Evidence from NHANES 2001-2008.Frontiers in nutrition · 2023Article
- Combined Dextran-Graft-Polyacrylamide/Zinc Oxide Nanocarrier for Effective Anticancer Therapy in vitro.International journal of nanomedicine · 2023Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cataracts are defined as the clouding of the lens due to the formation of insoluble protein aggregates. Metal ions exposure has been recognized as a risk factor in the cataract formation process. The γ and β crystallins are members of a larger family and share several structural features. Several studies have shown that copper and zinc ions induce the formation of γ-crystallins aggregates. However, the interaction of metal ions with β-crystallins, some of the most abundant crystallins in the lens, has not been explored until now. Here, we evaluate the effect of Cu(II) and Zn(II) ions on the aggregation of HβA1, as a representative of the acidic form, and HβB2, as a representative of the basic β-crystallins. We used several biophysical techniques and computational methods to show that Cu(II) and Zn(II) induce aggregation following different pathways. Both metal ions destabilize the proteins and impact protein folding. Copper induced a small conformational change in HβA1, leading to high-molecular-weight light-scattering aggregates, while zinc is more aggressive towards HβB2 and induces a larger conformational change. Our work provides information on the mechanisms of metal-induced aggregation of β-crystallins.
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