Editing Alpha-synuclein (section)

== Autoproteolytic activity ==

The use of high-resolution [[Ion-mobility spectrometry–mass spectrometry|ion-mobility mass spectrometry]] (IMS-MS) on HPLC-purified alpha-synuclein ''in vitro'' has shown alpha-synuclein to be [[autoproteolytic]] (self-[[Proteolysis|proteolytic]]), generating a variety of small [[molecular weight]] fragments upon incubation.<ref name="Vlad_2011">{{cite journal | vauthors = Vlad C, Lindner K, Karreman C, Schildknecht S, Leist M, Tomczyk N, Rontree J, Langridge J, Danzer K, Ciossek T, Petre A, Gross ML, Hengerer B, Przybylski M | title = Autoproteolytic fragments are intermediates in the oligomerization/aggregation of the Parkinson's disease protein alpha-synuclein as revealed by ion mobility mass spectrometry | journal = ChemBioChem | volume = 12 | issue = 18 | pages = 2740–2744 | date = December 2011 | pmid = 22162214 | pmc = 3461308 | doi = 10.1002/cbic.201100569 }}</ref> The 14.46&nbsp;[[Kilodalton|kDa]] protein was found to generate numerous smaller fragments, including 12.16&nbsp;kDa ([[amino acids]] 14–133) and 10.44&nbsp;kDa (40–140) fragments formed through [[C-terminus|C-]] and [[N-terminus|N-terminal]] truncation and a 7.27 kDa C-terminal fragment (72–140). The 7.27&nbsp;kDa fragment, which contains the majority of the NAC region, aggregated considerably faster than full-length alpha-synuclein. It is possible that these autoproteolytic products play a role as intermediates or cofactors in the aggregation of alpha-synuclein ''in vivo''.