ArticleCellular and molecular life sciences : CMLS2011
Transformation of amyloid β(1-40) oligomers into fibrils is characterized by a major change in secondary structure.
Article in Cellular and molecular life sciences : CMLS, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 147 citations in OpenAlex.
- Controlling Amyloid Assembly Dynamics Using Spin Interfaces.ACS nano · 2025Article
- Anti-amyloidogenic properties of 5‑caffeoylquinic acid-capped selenium nanoparticles.Scientific reports · 2025Article
- Development and validation of machine learning models with blood-based digital biomarkers for Alzheimer's disease diagnosis: a multicohort diagnostic study.EClinicalMedicine · 2025Article
- Fourier transform infrared spectroscopy detects distinct TAR DNA-binding protein 43 signatures in frontotemporal lobar degeneration.Frontiers in neuroscience · 2025Article
- Key considerations for ELISA-based quantification of diverse amyloid beta forms in murine brain homogenates.Frontiers in neuroscience · 2025Article
- Synchrotron radiation FTIR microspectroscopy enables measuring dynamic cell identity patterning during human 3D differentiation.Frontiers in cell and developmental biology · 2025Article
- Analysis of Conformational Molecular Changes in Cerebrospinal Fluid Using Fourier Transform Infrared Spectroscopy in Neurodegenerative Diseases.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Biofluid biomarkers for Alzheimer's disease: past, present, and future.Medical review (2021) · 2024Review
- Secondary Nucleation of Aβ Revealed by Single-Molecule and Computational Approaches.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- A turn for the worse: Aβ β-hairpins in Alzheimer's disease.Bioorganic & medicinal chemistry · 2024Review
- Hairpin trimer transition state of amyloid fibril.Nature communications · 2024Article
- Synthetic β-sheets mimicking fibrillar and oligomeric structures for evaluation of spectral X-ray scattering technique for biomarker quantification.Cell & bioscience · 2024Article
- Hfq C-terminal region forms a β-rich amyloid-like motif without perturbing the N-terminal Sm-like structure.Communications biology · 2023Article
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- Intermediate Antiparallel Fibrils in Aβ40 Dutch Mutant Aggregation: Insights from Nanoscale Infrared Spectroscopy.The journal of physical chemistry. B · 2023Article
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- Intermediate antiparallel fibrils in Aβ40 Dutch mutant aggregation: nanoscale insights from AFM-IR.bioRxiv : the preprint server for biology · 2023Article
- Aducanumab-Hope or Disappointment for Alzheimer's Disease.International journal of molecular sciences · 2023Review
- Selective In Vitro and Ex Vivo Staining of Brain Neurofibrillary Tangles and Amyloid Plaques by Novel Ethylene Ethynylene-Based Optical Sensors.Biosensors · 2023Article
- Article
8 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alzheimer's disease (AD) is a neurodegenerative disorder occurring in the elderly. It is widely accepted that the amyloid beta peptide (Aβ) aggregation and especially the oligomeric states rather than fibrils are involved in AD onset. We used infrared spectroscopy to provide structural information on the entire aggregation pathway of Aβ(1-40), starting from monomeric Aβ to the end of the process, fibrils. Our structural study suggests that conversion of oligomers into fibrils results from a transition from antiparallel to parallel β-sheet. These structural changes are described in terms of H-bonding rupture/formation, β-strands reorientation and β-sheet elongation. As antiparallel β-sheet structure is also observed for other amyloidogenic proteins forming oligomers, reorganization of the β-sheet implicating a reorientation of β-strands could be a generic mechanism determining the kinetics of protein misfolding. Elucidation of the process driving aggregation, including structural transitions, could be essential in a search for therapies inhibiting aggregation or disrupting aggregates.
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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.