논문 (학술지)
Competitive homo- and hetero- self-assembly of amyloid-beta 1-42 and 1-40 in the early stage of fibrillation
| 등록번호 | RPMS-2019-0190723633 | SCI 구분
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※구분 : SCI(SCIE포함), 비SCI |
SCI |
|---|---|---|---|
| 저자명 (주·공동저자) | Heo Chae Eun; Choi Tae Su; Kim Hugh I. | ||
| 논문구분 | 국외전문학술지 | 학술지명 | INTERNATIONAL JOURNAL OF MASS SPECTROMETRY |
| ISSN | 1387-3806 | 학술지 출판일자 | - |
| 학술지 볼륨번호 | 428 | 논문페이지 | 15 ~ 21 |
| 학술지 임팩트팩터 | 0.0 | 기여율 | 25 % |
| 초록 | Amyloid-β 1–42 (Aβ42) and 1–40 (Aβ40) peptides, whose self-assembly process has been linked with the formation of amyloid plaques in Alzheimer’s disease, exist as a mixture in human fluids. For this reason, heteromeric self-assembly of Aβ42 and Aβ40 has been widely investigated to understand the influence of this mixture in Aβ fibrillation. However, understanding the role of heteromeric self-assembly in Aβ fibrillation is a challenge owing to the heterogeneous cross-interactions between Aβ42 and Aβ40. Herein, we demonstrated the influence of the cross-interaction of Aβ42 and Aβ40 in the early stage of fibrillation using electrospray ionization mass spectrometry (ESI–MS) and drift tube ion mobility spectrometry (DTIMS) along with solution small-angle X-ray scattering (SAXS) and molecular dynamics (MD) simulations. In the mixture of Aβ42 and Aβ40, Aβ42 has only a slight preference for homo-oligomerization versus hetero-oligomerization with Aβ40 (∼1–2 fold) when forming small oligomers (from dimer to tetramer) in the early stage of fibrillation. However, the cross-interaction is gradually attenuated as oligomerization proceeds because of the different conformations in the Aβ42 and Aβ40 assemblies. Consequently, the competitive self-assembly of Aβ42 and Aβ40 can disturb the homo-oligomerization of Aβ42 in the early stage of fibrillation, whereas Aβ42 and Aβ40 species prefer the independent self-assembly after the early stage. | ||
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