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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Event Hall |
| Time |
4월 20일 (금요일) 11:00~12:30 |
| Code |
BIO.P-255 |
| Subject |
Direct AFM force mapping of single amyloid beta (Aβ) species to reveal characteristic of surface structure |
| Authors |
Jihyun Yoon, Joon Won Park*
Department of Chemistry, Pohang University of Science and Technology, Korea
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| Abstract |
Amyloid beta peptide (Aβ) is produced through sequential proteolytic cleavage of amyloid precursor protein (APP) which is a transmembrane protein by β- and γ- secretases. Aβ accumulation in human brain is considered to be an early toxic event in the pathogenesis of Alzheimer’s disease (AD) which is the most common cause of dementia. Currently, the pathological and physiological forms of Aβ, the structure of Aβ aggregates which is believed cause of AD and the mechanism of Aβ aggregation are not clear.
To characterize the structure and aggregation mechanism of Aβ species, we used AFM force mapping mode to investigate their surface structure at the molecular level. In this research, several models were set up to reveal surface structure of Aβ aggregates based on structural property of Aβ peptide. The structural models were as follow: 1) only N-terminus of Aβ exposed, 2) only C-terminus of Aβ exposed, 3) Both ends of Aβ exposed and 4) Both ends of Aβ unexposed. We used two different kinds of anti-Aβ probes in order to determine which model fits surface structure of Aβ aggregates. As a result, we observed specific interaction between Aβ and both C/N-terminal specific antibody suggests a surface structure model in which both N-terminus and C-terminus are exposed at the surface.
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| E-mail |
yoonjihyun@postech.ac.kr |
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121st General Meeting of the KCS