Disentangling aggregation-prone proteins: a new method for isolating α-synuclein species: An Editorial Highlight for "A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of α-synuclein monomers, oli
Disentangling aggregation-prone proteins: a new method for isolating α-synuclein species: An Editorial Highlight for "A simple, versatile and robust centrifugation-based filtration protocol for the isolation and quantification of α-synuclein monomers, oli
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解开易于聚集的蛋白质:一种分离 α-突触核蛋白种类的新方法:“一种简单、通用且强大的基于离心的过滤方案,用于分离和定量 α-突触核蛋白单体、oli
DOI:
10.1111/jnc.14973
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发表时间:
2020
影响因子:
4.7
通讯作者:
Nichols,MichaelR
中科院分区:
文献类型:
--
作者:
Nichols,MichaelR
Protein aggregation plays a central role in numerous neurodegenerative diseases. The key proteins in these diseases are of significant importance, but their investigation can be challenging due to unique properties of protein misfolding and oligomerization. Alpha‐synuclein protein (α‐Syn) is the predominant component of Lewy Bodies in Parkinson’s disease (PD) and is a member of this class of proteins. Many α‐Syn studies are limited by the inability to separate various monomeric, oligomeric, and fibrillar forms of the protein from heterogeneous mixtures. This Editorial Highlight summarizes the impact of a study published in the current issue of Journal of Neurochemistry, in which Lashuel and colleagues developed a simple, rapid centrifugation‐ and filter‐based method for separating, isolating, and quantifying different forms of α‐Syn. The researchers used electron microscopy, SDS‐PAGE, circular dichroism, and protein assays to carefully validate the method and quantitate α‐Syn yields and loss. The publication of this new method will not only aid in future studies of α‐Syn, but will likely extend to other proteins that underlie a variety of neurodegenerative diseases.