Insights into the mechanism of Alzheimer's β-amyloid aggregation as a function of concentration by using atomic force microscopy

Gina Mirela Mustata; Gajendra S. Shekhawat; Mary P. Lambert; Kirsten L. Viola; Pauline T. Velasco; William L. Klein; Vinayak P. Dravid

doi:10.1063/1.3697682

Insights into the mechanism of Alzheimer's β-amyloid aggregation as a function of concentration by using atomic force microscopy

Gina Mirela Mustata, Gajendra S. Shekhawat^*, Mary P. Lambert, Kirsten L. Viola, Pauline T. Velasco, William L. Klein, Vinayak P. Dravid

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

7 Scopus citations

Abstract

The size and shape of Alzheimer's β-amyloid structures, as well as the kinetics of their self-assembly, exhibits a very pronounced dependence on concentration and environment. In the present study, we are reporting the direct observation of Aβ oligomers and fibrils assemblies using atomic force microscopy imaging in fluid environment. These results demonstrate that in the Aβ preparations at lower concentrations, predominant are the globular, smaller oligomers, while for higher concentrations, globular oligomers co-exist with higher molecular weight fibrillar structures. At higher concentrations, the fibril formation is a dynamic and continuous process, yielding amyloid fibrils with multiple structures and diameters.

Original language	English (US)
Article number	133704
Journal	Applied Physics Letters
Volume	100
Issue number	13
DOIs	https://doi.org/10.1063/1.3697682
State	Published - Mar 26 2012

Funding

This work was supported by grants from the National Science Foundation Award Number EEC-0647560, CMMI-0926019, ECCS-0925882 and National Institutes of Health-National Institute on Aging Grants AG022547 and AG029460 (WLK). AFM imaging was performed in the NIFTI facility in the NUANCE center at Northwestern University, which is supported by NSF-NSEC, NSF-MRSEC, Keck Foundation, the State of Illinois, and Northwestern University.

ASJC Scopus subject areas

Physics and Astronomy (miscellaneous)

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10.1063/1.3697682

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title = "Insights into the mechanism of Alzheimer's β-amyloid aggregation as a function of concentration by using atomic force microscopy",

abstract = "The size and shape of Alzheimer's β-amyloid structures, as well as the kinetics of their self-assembly, exhibits a very pronounced dependence on concentration and environment. In the present study, we are reporting the direct observation of Aβ oligomers and fibrils assemblies using atomic force microscopy imaging in fluid environment. These results demonstrate that in the Aβ preparations at lower concentrations, predominant are the globular, smaller oligomers, while for higher concentrations, globular oligomers co-exist with higher molecular weight fibrillar structures. At higher concentrations, the fibril formation is a dynamic and continuous process, yielding amyloid fibrils with multiple structures and diameters.",

author = "Mustata, {Gina Mirela} and Shekhawat, {Gajendra S.} and Lambert, {Mary P.} and Viola, {Kirsten L.} and Velasco, {Pauline T.} and Klein, {William L.} and Dravid, {Vinayak P.}",

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AU - Velasco, Pauline T.

AU - Klein, William L.

AU - Dravid, Vinayak P.

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Insights into the mechanism of Alzheimer's β-amyloid aggregation as a function of concentration by using atomic force microscopy

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