Format

Send to

Choose Destination
FEBS Lett. 2015 Sep 14;589(19 Pt A):2640-8. doi: 10.1016/j.febslet.2015.07.013. Epub 2015 Jul 17.

Structural, morphological, and functional diversity of amyloid oligomers.

Author information

1
Department of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA. Electronic address: lbreydo@health.usf.edu.
2
Department of Molecular Medicine and Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA; Institute for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, Russian Federation; Department of Biology, Faculty of Science, King Abdulaziz University, P.O. Box 80203, Jeddah 21589, Saudi Arabia. Electronic address: vuversky@health.usf.edu.

Abstract

Protein misfolding and aggregation are known to play a crucial role in a number of important human diseases (Alzheimer's, Parkinson's, prion, diabetes, cataracts, etc.) as well as in a multitude of physiological processes. Protein aggregation is a highly complex process resulting in a variety of aggregates with different structures and morphologies. Oligomeric protein aggregates (amyloid oligomers) are formed as both intermediates and final products of the aggregation process. They are believed to play an important role in many protein aggregation-related diseases, and many of them are highly cytotoxic. Due to their instability and structural heterogeneity, information about structure, mechanism of formation, and physiological effects of amyloid oligomers is sparse. This review attempts to summarize the existing information on the major properties of amyloid oligomers.

KEYWORDS:

Amyloid fibril; Amyloid oligomer; Cytotoxicity; Protein aggregation; Protein misfolding

PMID:
26188543
DOI:
10.1016/j.febslet.2015.07.013
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center