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2 Nov 2009

Volume 95, Issue 18, Articles (18xxxx)

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Appl. Phys. Lett. 95, 183504 (2009); http://dx.doi.org/10.1063/1.3256223 (3 pages)

Hoon-Sik Kim, Sang Min Won, Young-Geun Ha, Jong-Hyun Ahn, Antonio Facchetti, Tobin J. Marks, and John A. Rogers
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Soluble state high resolution atomic force microscopy study of Alzheimer’s β-amyloid oligomers

Gajendra S. Shekhawat, Mary P. Lambert, Saurabh Sharma, Pauline T. Velasco, Kirsten L. Viola, William L. Klein, and Vinayak P. Dravid

Appl. Phys. Lett. 95, 183701 (2009); http://dx.doi.org/10.1063/1.3251779 (3 pages) | Cited 3 times

Online Publication Date: 6 November 2009

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We report here the direct observation of high resolution structures of assemblies of Alzheimer β-amyloid oligomers and monomers using liquid atomic force microscopy (AFM). Visualization of nanoscale features of Aβ oligomers (also known as ADDLs) was carried out in tapping mode AFM in F12 solution. Our results indicate that ADDL preparations exist in solution primarily as a mixture of monomeric peptides and higher molecular mass oligomers. Our study clearly reveals that the size and shape of these oligomer aggregates exhibit a pronounced dependence on concentration. These studies show that wet AFM enables direct assessment of oligomers in physiological fluids and suggests that this method may be developed to visualize Aβ oligomers from human fluids.
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87.64.Dz Scanning tunneling and atomic force microscopy
87.19.xr Degenerative diseases (Alzheimer's, ALS, etc)
87.14.ef Peptides
87.14.em Fibrils (amyloids, collagen, etc.)
87.15.bk Structure of aggregates
87.80.-y Biophysical techniques (research methods)
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