Disentangling aggregation‐prone proteins: a new method for isolating α‐synuclein species

Abstract

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.