ArticleJournal of the American Chemical Society2011
2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.
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Who cites it
59 citing papers in PubMed, 117 citations in OpenAlex.
- Dynamics of Solvating Water As a Probe of Polymers and Supramolecular Structures.Chemical reviews · 2026Review
- Mammals that can develop type 2 diabetes have a similarly structured β-sheet amyloid oligomer.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- O-glycosylated peptides curtail the aggregation and toxicity of human islet amyloid polypeptide.Communications biology · 2025Article
- Do selectivity filter carbonyls in KJournal of structural biology: X · 2024Article
- Water inside the Selectivity Filter of a KJournal of the American Chemical Society · 2024Article
- Probing the Hydrophobic Region of a Lipid Bilayer at Specific Depths Using Vibrational Spectroscopy.Journal of the American Chemical Society · 2023Article
- Probing Ion Configurations in the KcsA Selectivity Filter with Single-Isotope Labels and 2D IR Spectroscopy.Journal of the American Chemical Society · 2023Article
- In silico studies of the human IAPP in the presence of osmolytes.Journal of molecular modeling · 2022Article
- AIM: A Mapping Program for Infrared Spectroscopy of Proteins.Journal of chemical theory and computation · 2022Article
- Computational IR Spectroscopy of Insulin Dimer Structure and Conformational Heterogeneity.The journal of physical chemistry. B · 2021Article
- Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction.Chemical reviews · 2020Review
- d-Retro Inverso Amylin and the Stability of Amylin Fibrils.Journal of chemical theory and computation · 2020Article
- Non-Additive Effects of Binding Site Mutations in Calmodulin.Biochemistry · 2019Article
- Site-Specific Peptide Probes Detect Buried Water in a Lipid Membrane.Biophysical journal · 2019Article
- Vibrational Approach to the Dynamics and Structure of Protein Amyloids.Molecules (Basel, Switzerland) · 2019Review
- Structural Polymorphs Suggest Competing Pathways for the Formation of Amyloid Fibrils That Diverge from a Common Intermediate Species.Biochemistry · 2018Article
- Membranes as modulators of amyloid protein misfolding and target of toxicity.Biochimica et biophysica acta. Biomembranes · 2018Review
- Characterisation of the Structure and Oligomerisation of Islet Amyloid Polypeptides (IAPP): A Review of Molecular Dynamics Simulation Studies.Molecules (Basel, Switzerland) · 2018Review
- Role and Cytotoxicity of Amylin and Protection of Pancreatic Islet β-Cells from Amylin Cytotoxicity.Cells · 2018Review
- Structural Modulation of Human Amylin Protofilaments by Naturally Occurring Mutations.The journal of physical chemistry. B · 2018Article
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
Abstract
The aggregation of human amylin to form amyloid contributes to islet β-cell dysfunction in type 2 diabetes. Studies of amyloid formation have been hindered by the low structural resolution or relatively modest time resolution of standard methods. Two-dimensional infrared (2DIR) spectroscopy, with its sensitivity to protein secondary structures and its intrinsic fast time resolution, is capable of capturing structural changes during the aggregation process. Moreover, isotope labeling enables the measurement of residue-specific information. The diagonal line widths of 2DIR spectra contain information about dynamics and structural heterogeneity of the system. We illustrate the power of a combined atomistic molecular dynamics simulation and theoretical and experimental 2DIR approach by analyzing the variation in diagonal line widths of individual amide I modes in a series of labeled samples of amylin amyloid fibrils. The theoretical and experimental 2DIR line widths suggest a "W" pattern, as a function of residue number. We show that large line widths result from substantial structural disorder and that this pattern is indicative of the stable secondary structure of the two β-sheet regions. This work provides a protocol for bridging MD simulation and 2DIR experiments for future aggregation studies.
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