Binary Structure of Amyloid Beta Oligomers Revealed by Dual Recognition Mapping
Amyloid beta (Aβ) 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...
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| Veröffentlicht in: | Analytical chemistry (Washington) 2019-07, Vol.91 (13), p.8422-8428 |
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| creator | Yoon, Jihyun Kim, Youngkyu Park, Joon Won |
| description | Amyloid beta (Aβ) 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 Aβ40 and Aβ42 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 Aβ 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. |
| doi_str_mv | 10.1021/acs.analchem.9b01316 |
| format | Article |
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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 Aβ40 and Aβ42 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 Aβ peptides were recognized on the oligomer surface, and the termini detected pixel regions exhibited a lower elastic modulus than silent pixel regions. 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Chem</addtitle><description>Amyloid beta (Aβ) 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 Aβ40 and Aβ42 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 Aβ peptides were recognized on the oligomer surface, and the termini detected pixel regions exhibited a lower elastic modulus than silent pixel regions. 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| subjects | Alzheimer's disease Antibodies Atomic force microscopy C-Terminus Chemical compounds Chemistry Heterogeneity Mapping Mechanical properties Microscopy Modulus of elasticity Molecular structure Neurodegenerative diseases Oligomers Peptides Pharmacology Pixels |
| title | Binary Structure of Amyloid Beta Oligomers Revealed by Dual Recognition Mapping |
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