Journal
ANALYTICAL CHEMISTRY
Volume 91, Issue 13, Pages 8422-8428Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.analchem.9b01316
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Funding
- Basic Science Research Program through the National Research Foundation of Korea (NRF) - Ministry of Science, ICT and Future Planning [2017R1A2B3008478]
- Brain Research Program through the NRF - Ministry of Science, ICT and Future Planning [2015M3C7A1030964]
- National Research Foundation of Korea [2015M3C7A1030964, 2017R1A2B3008478] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Amyloid beta (A beta) oligomers are widely considered to be the causative agent of Alzheimer's disease (AD), a progressive neurodegenerative disorder. Determining the structure of oligomers is, therefore, important for understanding the disease and developing therapeutic agents; however, elucidating the structure has been proven difficult due to heterogeneity, noncrystallinity, and variability. Herein, we investigated homo-and hetero-oligomers of A beta 40 and A beta 42 using atomic force microscopy (AFM) and revealed characteristics of the molecular structure. By examining the surface of individual oligomers with sequential N- and C-terminus specific antibody-tethered tips, we simultaneously mapped the N- and C-terminus distributions and the elastic modulus. Interestingly, both the N- and C-termini of A beta peptides were recognized on the oligomer surface, and the termini detected pixel regions exhibited a lower elastic modulus than silent pixel regions. These two types of regions were randomly distributed on the oligomer surface.
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