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Cited by 184

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Solution State Characterization of Amyloid β-Derived Diffusible Ligands

Hepler, Robert W., Grimm, Karen M., Nahas, Deborah D., Breese, Robert, Dodson, Elizabeth Chen, Acton, Paul, Keller, Paul M., Yeager, Mark, Wang, Hui, Shughrue, Paul, Kinney, Gene, Joyce, Joseph G.·2006·Biochemistry
DOI 10.1021/bi061850f
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Abstract

A growing body of evidence suggests that soluble oligomeric forms of the amyloid beta peptide known as amyloid-derived diffusible ligands (ADDLs) are the toxic species responsible for neurodegeneration associated with Alzheimer's disease. Accurate biophysical characterization of ADDL preparations is hampered by the peptide's strong tendency to self-associate and the effect of factors such as ionic strength, temperature, and pH on its behavior. In addition, amyloid peptides are known to interact with common laboratory excipients, specifically detergents, further complicating the results from standard analytical methods such as denaturing polyacrylamide gel electrophoresis. We have studied the solution behavior of various amyloid peptide preparations using analytical ultracentrifugation and size exclusion chromatography coupled with multiangle laser light scattering. Our results indicate that ADDL preparations exist in solution primarily as a binary mixture of a monomeric peptide and high-molecular mass oligomers. We relate our findings to previously described characterizations utilizing atomic force microscopy and electrophoretic methods and demonstrate that low-molecular mass oligomers identified by gel electrophoresis likely represent artifacts induced by the peptide's interaction with detergent, while atomic force microscopy results are likely skewed by differential binding of monomeric and oligomeric peptide species. Finally, we confirm that only the high-molecular mass oligomeric components of an ADDL preparation are capable of binding to subpopulations of primary hippocampal neurons in vitro.

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Metadata

Authors
Hepler, R. W., Grimm, K. M., Nahas, D. D., Breese, R., Dodson, E. C., Acton, P., Keller, P. M., Yeager, M., Wang, H., Shughrue, P., Kinney, G., & Joyce, J. G.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2006-12-01
Volume
45
Issue
51
Pages
15157-15167
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi061850f
OpenAlex
W2093067743
Cited by
184
References
5
FWCI
8.04
Type
journal article
Language
en
Open access
closed

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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