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α-突触核蛋白纳米颗粒相互作用:构象可塑性的理解、控制和利用。

Alpha-Synuclein-Nanoparticle Interactions: Understanding, Controlling and Exploiting Conformational Plasticity.

机构信息

Department of Biotechnology, University of Verona, 37134 Verona, Italy.

出版信息

Molecules. 2020 Nov 29;25(23):5625. doi: 10.3390/molecules25235625.

Abstract

Alpha-synuclein (αS) is an extensively studied protein due to its involvement in a group of neurodegenerative disorders, including Parkinson's disease, and its documented ability to undergo aberrant self-aggregation resulting in the formation of amyloid-like fibrils. In dilute solution, the protein is intrinsically disordered but can adopt multiple alternative conformations under given conditions, such as upon adsorption to nanoscale surfaces. The study of αS-nanoparticle interactions allows us to better understand the behavior of the protein and provides the basis for developing systems capable of mitigating the formation of toxic aggregates as well as for designing hybrid nanomaterials with novel functionalities for applications in various research areas. In this review, we summarize current progress on αS-nanoparticle interactions with an emphasis on the conformational plasticity of the biomolecule.

摘要

α-突触核蛋白(αS)是一种广泛研究的蛋白质,因为它参与了一组神经退行性疾病,包括帕金森病,并且已经证明它有能力发生异常的自我聚集,导致形成类似淀粉样的纤维。在稀溶液中,该蛋白质本质上是无定形的,但在给定条件下可以采用多种替代构象,例如在吸附到纳米级表面时。研究αS-纳米颗粒相互作用可以帮助我们更好地理解蛋白质的行为,并为开发能够减轻有毒聚集体形成的系统以及设计具有新颖功能的混合纳米材料提供基础,这些材料可应用于各个研究领域。在这篇综述中,我们总结了目前关于αS-纳米颗粒相互作用的研究进展,重点介绍了生物分子的构象可塑性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/1685/7731430/5e4fbd8b67d4/molecules-25-05625-g001.jpg

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