ArticleProtein science : a publication of the Protein Society2025
Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.
Article in Protein science : a publication of the Protein Society, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
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- Metal Ion-Specific Modulation of Network Connectivity and Defects in Poly(ethylene glycol)-Peptide Conjugate Assemblies and Hydrogels.Chemistry of materials : a publication of the American Chemical Society · 2026Article
- Spectroscopic and calorimetric analysis of the interaction between 9-hydroxy-5-methyl-12Frontiers in molecular biosciences · 2026Article
- Advances in Synchrotron Radiation-Based Vacuum-Ultraviolet Circular Dichroism for Biomolecular Structural Analysis.Chemistry, an Asian journal · 2026Review
- Developing Subcutaneous Formulations for Irisin as a Potential Therapeutic.Pharmaceutical research · 2025Article
- Evaluation of Mannitol's Crystallization Impact on the Secondary Structure of Spray-Dried recombinant human Growth Hormone (rhGH) Formulations.Pharmaceutical research · 2025Article
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- Anionic Lipid Catalyzes the Generation of Cytotoxic Insulin Oligomers.Biomolecules · 2025Article
- BeStSel: analysis site for protein CD spectra-2025 update.Nucleic acids research · 2025Article
- Improving the solubility of single domain antibodies using VH-like hallmark residues.Protein science : a publication of the Protein Society · 2025Article
- Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025Review
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Authors and funding
11 authors.
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Abstract
Protein aggregation and amyloid formation are linked to numerous degenerative diseases, such as Alzheimer's or Parkinson's disease. Additionally, protein aggregation plays a crucial role in various biological processes, such as storage of molecules or cell signaling. Protein molecules can form a wide range of aggregates, from oligomers of different sizes to non-specific aggregates and highly ordered cross-β structured amyloid fibrils with diverse morphologies. Circular dichroism (CD) spectroscopy is a widely used technique to study protein structures providing detailed information at the secondary structure level, and is ideal to distinguish and characterize protein aggregates. Despite its potential, CD spectroscopy is often perceived as having limited application on protein aggregates due to challenges, such as sample inhomogeneity, precipitation, light scattering and other factors that complicate accurate analysis. In this study, we present a detailed protocol for examining the structure of protein aggregates and amyloid fibrils using CD spectroscopy. We outline the optimal experimental conditions for sample preparation and demonstrate how to identify and mitigate various interfering effects, using specific examples of disease-related amyloidogenic proteins. We also discuss the instrumental parameters, baseline subtraction, normalization, and quality control of CD spectra. Furthermore, we evaluate the performance of different secondary structure estimating algorithms on amyloid fibril CD spectra highlighting the superiority of BeStSel and CDNN. Our findings could enhance the structural analysis of protein aggregates, contributing to a better understanding of associated diseases and the development of new therapeutic strategies.
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