ArticleProceedings of the National Academy of Sciences of the United States of America2010
Discriminating early stage A{beta}42 monomer structures using chirality-induced 2DIR spectroscopy in a simulation study.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Biophysical insights into the molecular mechanisms of beta amyloid aggregation and its toxic effects in Alzheimer's disease.Frontiers in molecular biosciences · 2025Review
- Distinctive contribution of two additional residues in protein aggregation of Aβ42 and Aβ40 isoforms.BMB reports · 2024Review
- Applications of Single-Molecule Vibrational Spectroscopic Techniques for the Structural Investigation of Amyloid Oligomers.Molecules (Basel, Switzerland) · 2022Review
- Racemization in Post-Translational Modifications Relevance to Protein Aging, Aggregation and Neurodegeneration: Tip of the Iceberg.Symmetry · 2021Article
- Article
- Impact of Mutations on the Conformational Transition from α-Helix to β-Sheet Structures in Arctic-Type AβACS omega · 2020Article
- A Proposed Method to Obtain Surface Specificity with Pump-Probe and 2D Spectroscopies.The journal of physical chemistry. A · 2020Article
- 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
- Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.The journal of physical chemistry. B · 2013Article
- Deducing conformational variability of intrinsically disordered proteins from infrared spectroscopy with Bayesian statistics.Chemical physics · 2013Article
- Monitoring the folding of Trp-cage peptide by two-dimensional infrared (2DIR) spectroscopy.The journal of physical chemistry. B · 2013Article
- Tracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopy.The journal of physical chemistry. A · 2013Article
- Spectroscopic studies of protein folding: linear and nonlinear methods.Protein science : a publication of the Protein Society · 2012Review
- Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy.The journal of physical chemistry. B · 2011Article
- Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences.Angewandte Chemie (International ed. in English) · 2010Article
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5 authors.
Funding
Abstract
Elucidating the structural features of the Abeta monomer, the peptide constituent of amyloid fibrils found in Alzheimer's disease, can enable a direct characterization of aggregation pathways. Recent studies support the view that the ensemble of Abeta42 monomers is a mixture of diverse ordered and disordered conformational species, which can be classified according to the formation of a characteristic beta-hairpin conformation in a certain region. Despite the disparity in the structural features of these species, commonly used spectroscopic techniques such as NMR may not directly trace the conformational dynamics in the ensemble due to the limited time resolution and the lack of well-resolved spectral features for different comformers. Here we use molecular dynamics simulations combined with simulations of two-dimensional IR (2DIR) spectra to investigate the structure of these species, their interchange kinetics, and their spectral features. We show that while the discrimination efficiency of the ordinary, nonchiral 2DIR signal is limited due to its intrinsic dependence on common order parameters that are dominated by the generally unstructured part of the sequence, signals with carefully designed chirality-sensitive pulse configurations have the high resolution required for differentiating the various monomer structures. Our combined simulation studies indicate the power of the chirality-induced (CI) 2DIR technique in investigating early events in Abeta42 aggregation and open the possibility for their use as a novel experimental tool.
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