ArticlePloS one2011
αA-crystallin peptide SDRDKFVIFLDVKHF accumulating in aging lens impairs the function of α-crystallin and induces lens protein aggregation.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 60 citations in OpenAlex.
- Reversing the Fold: Polyanionic Macrocycle Dissolves αA66-80 Crystallin Peptide Aggregates.Biomacromolecules · 2026Article
- Lens aging and disease: Molecular mechanisms, functional consequences, and pharmacological implications.Progress in retinal and eye research · 2026Review
- Identification of Age- and Cataract-Related Changes in High-Density Lens Protein Aggregates.Investigative ophthalmology & visual science · 2025Article
- Cholesterol and Q147E Deamidation Modulates αA-Crystallin Membrane Binding Elucidating Protective Role of Lens Membrane Composition Changes With Aging.Investigative ophthalmology & visual science · 2025Article
- Cholesterol Content Regulates the Interaction of αA-, αB-, and α-Crystallin with the Model of Human Lens-Lipid Membranes.International journal of molecular sciences · 2024Article
- The Role of Gap Junctions Dysfunction in the Development of Cataracts: From Loss of Cell-to-Cell Transfer to Blurred Vision-Review.Bioelectricity · 2023Review
- Expression of miR-210-3p in the aqueous humor of patients with age-related cataracts and its effect on human lens epithelial cell injury induced by hydrogen peroxide.Arquivos brasileiros de oftalmologia · 2023Article
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- αA and αB peptides from human cataractous lenses show antichaperone activity and enhance aggregation of lens proteins.Molecular vision · 2022Article
- Functionalized resorcinarenes effectively disrupt the aggregation of αA66-80 crystallin peptide related to cataracts.RSC medicinal chemistry · 2021Article
- Acceleration of age-induced proteolysis in the guinea pig lens nucleus by in vivo exposure to hyperbaric oxygen: A mass spectrometry analysis.Experimental eye research · 2021Article
- Aggregation of gelsolin wild-type and G167K/R, N184K, and D187N/Y mutant peptides and inhibition.Molecular and cellular biochemistry · 2021Article
- α-Crystallins in the Vertebrate Eye Lens: Complex Oligomers and Molecular Chaperones.Annual review of physical chemistry · 2021Review
- Interaction of Alpha-Crystallin with Phospholipid Membranes.Current eye research · 2021Article
- Isomerization of Asp is essential for assembly of amyloid-like fibrils of αA-crystallin-derived peptide.PloS one · 2021Article
- Interaction of alpha-crystallin with four major phospholipids of eye lens membranes.Experimental eye research · 2021Article
- Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens.The protein journal · 2020Article
- Current Trends in the Pharmacotherapy of Cataracts.Pharmaceuticals (Basel, Switzerland) · 2020Review
- Development of a brain-permeable peptide nanofiber that prevents aggregation of Alzheimer pathogenic proteins.PloS one · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe eye lens is composed of fiber cells that are filled with α-, β- and γ-crystallins. The primary function of crystallins is to maintain the clarity of the lens through ordered interactions as well as through the chaperone-like function of α-crystallin. With aging, the chaperone function of α-crystallin decreases, with the concomitant accumulation of water-insoluble, light-scattering oligomers and crystallin-derived peptides. The role of crystallin-derived peptides in age-related lens protein aggregation and insolubilization is not understood. METHODOLOGY/PRINCIPAL
findingsWe found that αA-crystallin-derived peptide, (66)SDRDKFVIFLDVKHF(80), which accumulates in the aging lens, can inhibit the chaperone activity of α-crystallin and cause aggregation and precipitation of lens crystallins. Age-related change in the concentration of αA-(66-80) peptide was estimated by mass spectrometry. The interaction of the peptide with native crystallin was studied by multi-angle light scattering and fluorescence methods. High molar ratios of peptide-to-crystallin were favourable for aggregation and precipitation. Time-lapse recordings showed that, in the presence of αA-(66-80) peptide, α-crystallin aggregates and functions as a nucleus for protein aggregation, attracting aggregation of additional α-, β- and γ-crystallins. Additionally, the αA-(66-80) peptide shares the principal properties of amyloid peptides, such as β-sheet structure and fibril formation. CONCLUSIONS/SIGNIFICANCE: These results suggest that crystallin-derived peptides such as αA-(66-80), generated in vivo, can induce age-related lens changes by disrupting the structure and organization of crystallins, leading to their insolubilization. The accumulation of such peptides in aging lenses may explain a novel mechanism for age-related crystallin aggregation and cataractogenesis.
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Registered trials
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.