Cited by 118Alzheimer's disease research and treatmentsMass Spectrometry Techniques and ApplicationsAdvanced Proteomics Techniques and Applications

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Pulsed hydrogen–deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation

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Zhang, Ying, Rempel, Don L., Zhang, Jun, Sharma, Anuj K., Mirica, Liviu M., Gross, Michael L.·2013·Proceedings of the National Academy of Sciences

DOI 10.1073/pnas.1309175110PMC PMC3767558

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Abstract

Probing the conformational changes of amyloid beta (Aβ) peptide aggregation is challenging owing to the vast heterogeneity of the resulting soluble aggregates. To investigate the formation of these aggregates in solution, we designed an MS-based biophysical approach and applied it to the formation of soluble aggregates of the Aβ42 peptide, the proposed causative agent in Alzheimer's disease. The approach incorporates pulsed hydrogen-deuterium exchange coupled with MS analysis. The combined approach provides evidence for a self-catalyzed aggregation with a lag phase, as observed previously by fluorescence methods. Unlike those approaches, pulsed hydrogen-deuterium exchange does not require modified Aβ42 (e.g., labeling with a fluorophore). Furthermore, the approach reveals that the center region of Aβ42 is first to aggregate, followed by the C and N termini. We also found that the lag phase in the aggregation of soluble species is affected by temperature and Cu(2+) ions. This MS approach has sufficient structural resolution to allow interrogation of Aβ aggregation in physiologically relevant environments. This platform should be generally useful for investigating the aggregation of other amyloid-forming proteins and neurotoxic soluble peptide aggregates.

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Authors: Zhang, Y., Rempel, D. L., Zhang, J., Sharma, A. K., Mirica, L. M., & Gross, M. L.
Affiliations: California Institute of Technology (US)
ORCID: Zhang, Ying
Rempel, Don L.
Zhang, Jun
Sharma, Anuj K.
Mirica, Liviu M.
Gross, Michael L.
Venue: Proceedings of the National Academy of Sciences
Publisher: National Academy of Sciences
Published: 2013-08-19
Volume: 110
Issue: 36
Pages: 14604-14609
ISSN: 0027-8424 (ISSN-L)
1091-6490
DOI: 10.1073/pnas.1309175110
PMC: PMC3767558
OpenAlex: W2165610594
Cited by: 118
References: 71
Citations by year: 2026: 1 · 2025: 5 · 2024: 4 · 2023: 12 · 2022: 10 · 2021: 7 · 2020: 14 · 2019: 9 · 2018: 12 · 2017: 7 · 2016: 8 · 2015: 12 · 2014: 13 · 2013: 4
FWCI: 8.59
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Proceedings of the National Academy of Sciences (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Alzheimer's Association (AG05681, NIRP-12-259199, 12-259199)
Oak Ridge Associated Universities
National Institutes of Health (GM103422, AG05681)
Charles F. and Joanne Knight Alzheimer Disease Research Center, Washington University in St. Louis (P50 AG0568 1)
National Institute on Aging (P 50 AG05681, P50AG005681)
National Institute of General Medical Sciences (GM103422, P41GM103422)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Physical Sciences › Chemistry › Spectroscopy › Mass Spectrometry Techniques and Applications
Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
Keywords: amyloid-beta, amyloid-beta 42, peptide aggregation, hydrogen-deuterium exchange, conformational change, lag phase, Alzheimer's disease, copper ions, temperature effects
MeSH terms: Alzheimer Disease, Amyloid, Copper, Deuterium, Humans, Hydrogen, Peptide Fragments, Protein Conformation, Mass Spectrometry, Temperature, Blotting, Western, Amyloid beta-Peptides, Deuterium Exchange Measurement, Microscopy, Electron, Transmission

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Pulsed hydrogen–deuterium exchange mass spectrometry probes conformational changes in amyloid beta (Aβ) peptide aggregation

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