Structural Differences Between Amyloid Beta Oligomers

Authors

Leonid Breydo, University of California
Dmitry Kurouski, University at Albany
Suhail Rasool, University of California
Saskia Milton, University of California
Jessica W. Wu, University of California
Vladimir N. Uversky, University of South FloridaFollow
Igor K. Lednev, University at Albany
Charles G. Glabe, University of California

Document Type

Article

Publication Date

2016

Digital Object Identifier (DOI)

https://doi.org/10.1016/j.bbrc.2016.06.122

Abstract

In Alzheimer’s disease, soluble Aβ oligomers are believed to play important roles in the disease pathogenesis, and their levels correlate with cognitive impairment. We have previously shown that Aβ oligomers can be categorized into multiple structural classes based on their reactivity with conformation-dependent antibodies. In this study, we analyzed the structures of Aβ40 oligomers belonging to two of these classes: fibrillar and prefibrillar oligomers. We found that fibrillar oligomers were similar in structure to fibrils but were less stable towards denaturation while prefibrillar oligomers were found to be partially disordered. These results are consistent with previously proposed structures for both oligomer classes while providing additional structural information.

Was this content written or created while at USF?

Yes

Citation / Publisher Attribution

Biochemical and Biophysical Research Communications, v. 477, issue 4, p. 700-705

Scholar Commons Citation

Breydo, Leonid; Kurouski, Dmitry; Rasool, Suhail; Milton, Saskia; Wu, Jessica W.; Uversky, Vladimir N.; Lednev, Igor K.; and Glabe, Charles G., "Structural Differences Between Amyloid Beta Oligomers" (2016). Molecular Medicine Faculty Publications. 362.
https://digitalcommons.usf.edu/mme_facpub/362