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Biochem Biophys Res Commun. 2016 Sep 2;477(4):700-705. doi: 10.1016/j.bbrc.2016.06.122. Epub 2016 Jun 27.

Structural differences between amyloid beta oligomers.

Author information

1
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States. Electronic address: lbreydo@health.usf.edu.
2
Department of Chemistry, University at Albany, SUNY, 1400 Washington Avenue, Albany, NY 12222, United States.
3
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States.
4
Department of Molecular Medicine and Byrd Alzheimer's Institute, University of South Florida, Tampa, FL 33612, United States; Department of Biological Sciences, Faculty of Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.
5
Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, United States; Biochemistry Department, Faculty of Science and Experimental Biochemistry Unit, King Fahd Medical Research Center, King Abdulaziz University, Jeddah, Saudi Arabia.

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.

KEYWORDS:

Alzheimer’s disease; Amyloid beta; Oligomers; Protein aggregation

PMID:
27363332
DOI:
10.1016/j.bbrc.2016.06.122
[Indexed for MEDLINE]

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