Graduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA.
Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, USA.
Biomolecules. 2023 Oct 2;13(10):1476. doi: 10.3390/biom13101476.
The small neuronal protein α-synuclein (αS) is found in pre-synaptic terminals and plays a role in vesicle recycling and neurotransmission. Fibrillar aggregates of αS are the hallmark of Parkinson's disease and related neurodegenerative disorders. In both health and disease, interactions with lipids influence αS's structure and function, prompting much study of the effects of lipids on αS aggregation. A comprehensive collection (126 examples) of aggregation rate data for various αS/lipid combinations was presented, including combinations of lipid variations and mutations or post-translational modifications of αS. These data were interpreted in terms of lipid structure to identify general trends. These tabulated data serve as a resource for the community to help in the interpretation of aggregation experiments with lipids and to be potentially used as inputs for computational models of lipid effects on aggregation.
小神经元蛋白α-突触核蛋白(αS)存在于突触前末梢,在囊泡循环和神经递质传递中发挥作用。αS 的纤维状聚集物是帕金森病和相关神经退行性疾病的标志。在健康和疾病状态下,与脂质的相互作用影响 αS 的结构和功能,这促使人们对脂质对 αS 聚集的影响进行了大量研究。本文汇总了各种 αS/脂质组合的聚集速率数据(共 126 个实例),包括脂质变化与 αS 突变或翻译后修饰的组合。根据脂质结构对这些数据进行了解释,以确定一般趋势。这些表格化的数据为研究人员提供了一个资源,有助于解释脂质对聚集实验的影响,并有可能被用作计算模型中脂质对聚集影响的输入。