Thermodynamics of oligomerization and Helix-to-sheet structural transition of amyloid β-protein on anionic phospholipid vesicles

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Biophysical chemistry Pub Date : 2024-04-18 DOI:10.1016/j.bpc.2024.107248
Keisuke Ikeda, Yuuki Sugiura, Hiroyuki Nakao, Minoru Nakano
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Abstract

Understanding oligomerization and aggregation of the amyloid-β protein is important to elucidate the pathological mechanisms of Alzheimer's disease, and lipid membranes play critical roles in this process. In addition to studies reported by other groups, our group has also reported that the negatively-charged lipid bilayers with a high positive curvature induced α-helix-to-β-sheet conformational transitions of amyloid-β-(1–40) upon increase in protein density on the membrane surface and promoted amyloid fibril formation of the protein. Herein, we investigated detailed mechanisms of the conformational transition and oligomer formation of the amyloid-β protein on the membrane surface. Changes in the fractions of the three protein conformers (free monomer, membrane-bound α-helix-rich conformation, and β-sheet-rich conformation) were determined from the fluorescent spectral changes of the tryptophan probe in the protein. The helix-to-sheet structural transition on the surface was described by a thermodynamic model of octamer formation driven by entropic forces including hydrophobic interactions. These findings provide useful information for understanding the self-assembly of amyloidogenic proteins on lipid membrane surfaces.

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淀粉样β蛋白在阴离子磷脂囊泡上的寡聚化和螺旋到片状结构转变的热力学研究
了解淀粉样β蛋白的寡聚和聚集对于阐明阿尔茨海默病的病理机制非常重要,而脂质膜在这一过程中起着关键作用。除了其他研究小组的研究外,我们小组还报道了高正曲率的带负电荷脂质双层膜在膜表面蛋白质密度增加时诱导淀粉样-β-(1-40)的α-螺旋到β-片构象转变,并促进蛋白质的淀粉样纤维形成。在此,我们研究了淀粉样-β蛋白在膜表面构象转变和寡聚体形成的详细机制。根据蛋白质中色氨酸探针的荧光光谱变化,确定了三种蛋白质构象(游离单体、膜结合的富含α-螺旋构象和富含β-片层构象)组分的变化。八聚体形成的热力学模型描述了表面从螺旋到片状的结构转变,该模型由包括疏水相互作用在内的熵力驱动。这些发现为理解淀粉样蛋白在脂膜表面的自组装提供了有用的信息。
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来源期刊
Biophysical chemistry
Biophysical chemistry 生物-生化与分子生物学
CiteScore
6.10
自引率
10.50%
发文量
121
审稿时长
20 days
期刊介绍: Biophysical Chemistry publishes original work and reviews in the areas of chemistry and physics directly impacting biological phenomena. Quantitative analysis of the properties of biological macromolecules, biologically active molecules, macromolecular assemblies and cell components in terms of kinetics, thermodynamics, spatio-temporal organization, NMR and X-ray structural biology, as well as single-molecule detection represent a major focus of the journal. Theoretical and computational treatments of biomacromolecular systems, macromolecular interactions, regulatory control and systems biology are also of interest to the journal.
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