ArticleJournal of the American Chemical Society2012
Structure and composition of insulin fibril surfaces probed by TERS.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 167 citations in OpenAlex.
- Bioanalysis Using Surface-Enhanced Raman Spectroscopy: From the Perspective of Single Molecules.ACS nano · 2026Review
- Exploring collagen fibrillogenesis at the nanoscale: Tip-enhanced Raman imaging of protofibrils.Journal of microscopy · 2026Article
- Molecular states and interfacial interactions at solid-liquid interfaces: advances and challenges in multimodal characterization.Beilstein journal of nanotechnology · 2026Review
- The Catalyzing Effect of Aggregates on the Fibrillation Pathway of Human Insulin: A Spectroscopic Investigation During the Lag Phase.International journal of molecular sciences · 2025Article
- Unravelling emergence of chirality in click-chemistry polymers down to the single-chain level.Nature communications · 2025Article
- Secondary structure and toxicity of lysozyme fibrils are determined by the length and unsaturation of phosphatidic acid.Proteins · 2024Article
- Long-Chain Polyunsaturated Fatty Acids Accelerate the Rate of Insulin Aggregation and Enhance Toxicity of Insulin Aggregates.ACS chemical neuroscience · 2024Article
- Concentration of Phosphatidylserine Influence Rates of Insulin Aggregation and Toxicity of Amyloid Aggregates In Vitro.ACS chemical neuroscience · 2023Article
- Lipids uniquely alter rates of insulin aggregation and lower toxicity of amyloid aggregates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023Article
- Amyloid aggregates exert cell toxicity causing irreversible damages in the endoplasmic reticulum.Biochimica et biophysica acta. Molecular basis of disease · 2022Article
- Molecular Aspects of Insulin Aggregation and Various Therapeutic Interventions.ACS bio & med chem Au · 2022Review
- The degree of unsaturation of fatty acids in phosphatidylserine alters the rate of insulin aggregation and the structure and toxicity of amyloid aggregates.FEBS letters · 2022Article
- Unsaturation in the Fatty Acids of Phospholipids Drastically Alters the Structure and Toxicity of Insulin Aggregates Grown in Their Presence.The journal of physical chemistry letters · 2022Article
- Challenges in Experimental Methods.Methods in molecular biology (Clifton, N.J.) · 2022Article
- UV Resonance Raman explores protein structural modification upon fibrillation and ligand interaction.Biophysical journal · 2021Article
- Infrared and Raman chemical imaging and spectroscopy at the nanoscale.Chemical Society reviews · 2020Article
- Molecular Spectroscopic Markers of Abnormal Protein Aggregation.Molecules (Basel, Switzerland) · 2020Review
- Surface Enhanced Raman Scattering Selectivity in Proteins Arises from Electron Capture and Resonant Enhancement of Radical Species.The journal of physical chemistry. C, Nanomaterials and interfaces · 2020Article
- Present and Future of Surface-Enhanced Raman Scattering.ACS nano · 2020Article
- Noncontact tip-enhanced Raman spectroscopy for nanomaterials and biomedical applications.Nanoscale advances · 2019Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Amyloid fibrils associated with many neurodegenerative diseases are the most intriguing targets of modern structural biology. Significant knowledge has been accumulated about the morphology and fibril-core structure recently. However, no conventional methods could probe the fibril surface despite its significant role in the biological activity. Tip-enhanced Raman spectroscopy (TERS) offers a unique opportunity to characterize the surface structure of an individual fibril due to a high depth and lateral spatial resolution of the method in the nanometer range. Herein, TERS is utilized for characterizing the secondary structure and amino acid residue composition of the surface of insulin fibrils. It was found that the surface is strongly heterogeneous and consists of clusters with various protein conformations. More than 30% of the fibril surface is dominated by β-sheet secondary structure, further developing Dobson's model of amyloid fibrils (Jimenez et al. Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 9196-9201). The propensity of various amino acids to be on the fibril surface and specific surface secondary structure elements were evaluated. β-sheet areas are rich in cysteine and aromatic amino acids, such as phenylalanine and tyrosine, whereas proline was found only in α-helical and unordered protein clusters. In addition, we showed that carboxyl, amino, and imino groups are nearly equally distributed over β-sheet and α-helix/unordered regions. Overall, this study provides valuable new information about the structure and composition of the insulin fibril surface and demonstrates the power of TERS for fibril characterization.
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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.