논문 (학술지)
Electrostatic and hydrophobic interactions of lipid-associated alpha synuclein: The role of a water-limited interfaces in amyloid fibrillation
| 등록번호 | RPMS-2019-0190739514 | SCI 구분
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※구분 : SCI(SCIE포함), 비SCI |
SCI |
|---|---|---|---|
| 저자명 (주·공동저자) | Choi Tae Su; Han Jong Yoon; Heo Chae Eun; Lee Sun Woo; Kim Hugh I. | ||
| 논문구분 | 국외전문학술지 | 학술지명 | BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES |
| ISSN | 0005-2736 | 학술지 출판일자 | - |
| 학술지 볼륨번호 | 1860 | 논문페이지 | 1854 ~ 1862 |
| 학술지 임팩트팩터 | 0.0 | 기여율 | 33 % |
| 초록 | Human α‑synuclein (αSyn) is an intrinsically disordered protein (IDP) whose biological and pathological functions in brain neuronal cells have not yet been fully elucidated. αSyn intrinsically participates in aiding neurotransmitter trafficking through αSyn the association with lipid membranes. However, lipid-associated states of αSyn also induce amyloid self-assembly that is linked to the pathogenesis of various synucleinopathies. These contradicting actions arise from the limited water content near lipid-water interfaces that controls αSyn electrostatic and hydrophobic interactions. Thus, understanding the molecular interactions between αSyn and lipid membranes in the presence of water molecules is critical in elucidating the pivotal role of lipid-associated αSyn in amyloid self-assembly. In this review, we describe how the membrane interface controls electrostatic and hydrophobic interactions of lipid-associated αSyn. Moreover, membrane amyloid self-assembly of αSyn will be further discussed with regards to the structural dynamics of lipid-associated αSyn and water molecules near the interface. | ||
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