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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Zhang, Ying Rempel, Don L. Mirica, Liviu M. Sharma, Anuj K. Zhang, Jun Gross, Michael L. |
| Description | Author Affiliation: Zhang Y ( Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130, USA.); |
| 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 $Aβ_{42}$ 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 $Aβ_{42}$ (e.g., labeling with a fluorophore). Furthermore, the approach reveals that the center region of $Aβ_{42}$ 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 36 |
| Volume Number | 110 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2013-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Amyloid Beta-Peptides Chemistry Deuterium Exchange Measurement Mass Spectrometry Protein Conformation Alzheimer Disease Metabolism Amyloid Ultrastructure Blotting, Western Copper Deuterium Hydrogen Microscopy, Electron, Transmission Peptide Fragments Temperature Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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