ArticleJournal of molecular biology2017
Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.
Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 38 citations in OpenAlex.
- Multidimensional Infrared Spectroscopy as a Bioanalytical Technique.Chemical reviews · 2026Review
- UV light and the ocular lens: a review of exposure models and resulting biomolecular changes.Frontiers in ophthalmology · 2024Review
- Simultaneously Measured Kinetics of Two Amyloid Polymorphs Using Cross Peak Specific 2D IR Spectroscopy.The journal of physical chemistry letters · 2023Article
- Design and Characterization of Model Systems that Promote and Disrupt Transparency of Vertebrate Crystallins In Vitro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Investigating Chaperone like Activity of Green Silver Nanoparticles: Possible Implications in Drug Development.Molecules (Basel, Switzerland) · 2022Article
- Application of 2D IR Bioimaging: Hyperspectral Images of Formalin-Fixed Pancreatic Tissues and Observation of Slow Protein Degradation.The journal of physical chemistry. B · 2021Article
- Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- UV Effect on Human Anterior Lens Capsule Macro-Molecular Composition Studied by Synchrotron-Based FTIR Micro-Spectroscopy.International journal of molecular sciences · 2021Article
- Chemical Properties Determine Solubility and Stability in βγ-Crystallins of the Eye Lens.Chembiochem : a European journal of chemical biology · 2021Review
- Article
- Mechanism of human γD-crystallin protein aggregation in UV-C light.Molecular vision · 2021Article
- Trehalose Inhibits the Heat-Induced Formation of the Amyloid-Like Structure of Soluble Proteins Isolated from Human Cataract Lens.The protein journal · 2020Article
- Function and Aggregation in Structural Eye Lens Crystallins.Accounts of chemical research · 2020Review
- Amyloid found in human cataracts with two-dimensional infrared spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Determination of the Solution Structure of Antifreeze Glycoproteins Using Two-Dimensional Infrared Spectroscopy.The journal of physical chemistry letters · 2019Article
- RETRACTED: Peptide-induced formation of protein aggregates and amyloid fibrils in human and guinea pig αA-crystallins under physiological conditions of temperature and pH.Experimental eye research · 2019Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
- Two-Dimensional Spectroscopy Is Being Used to Address Core Scientific Questions in Biology and Materials Science.The journal of physical chemistry. B · 2018Review
- Not All β-Sheets Are the Same: Amyloid Infrared Spectra, Transition Dipole Strengths, and Couplings Investigated by 2D IR Spectroscopy.The journal of physical chemistry. B · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cataracts are formed by the aggregation of crystallin proteins in the eye lens. Many in vitro studies have established that crystallin proteins precipitate into aggregates that contain amyloid fibers when denatured, but there is little evidence that ex vivo cataracts contain amyloid. In this study, we collect two-dimensional infrared (2D IR) spectra on tissue slices of porcine eye lenses. As shown in control experiments on in vitro αB- and γD-crystallin, 2D IR spectroscopy can identify the highly ordered β-sheets typical of amyloid secondary structure even if the fibers themselves are too short to be resolved with TEM. In ex vivo experiments of acid-treated tissues, characteristic 2D IR features are observed and fibers >50nm in length are resolved by transmission electron microscopy (TEM), consistent with amyloid fibers. In UV-irradiated lens tissues, fibers are not observed with TEM, but highly ordered β-sheets of amyloid secondary structure is identified from the 2D IR spectra. The characteristic 2D IR features of amyloid β-sheet secondary structure are created by as few as four or five strands and so identify amyloid secondary structure even if the aggregates themselves are too small to be resolved with TEM. We discuss these findings in the context of the chaperone system of the lens, which we hypothesize sequesters small aggregates, thereby preventing long fibers from forming. This study expands the scope of heterodyned 2D IR spectroscopy to tissues. The results provide a link between in vitro and ex vivo studies and support the hypothesis that cataracts are an amyloid disease.
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