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Biomolecules 2015, 5(3), 1210-1227; doi:10.3390/biom5031210

Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications

Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA
Department of Molecular and Computational Biology, University of Southern California, Los Angeles, CA 90089, USA
Author to whom correspondence should be addressed.
Academic Editor: Stephan N. Witt
Received: 17 March 2015 / Revised: 17 May 2015 / Accepted: 9 June 2015 / Published: 25 June 2015
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α-Synuclein is the aggregation-prone protein associated with Parkinson’s disease (PD) and related neurodegenerative diseases. Complicating both its biological functions and toxic aggregation are a variety of posttranslational modifications. These modifications have the potential to either positively or negatively affect α-synuclein aggregation, raising the possibility that the enzymes that add or remove these modifications could be therapeutic targets in PD. Synthetic protein chemistry is uniquely positioned to generate site-specifically and homogeneously modified proteins for biochemical study. Here, we review the application of synthetic peptides and proteins towards understanding the effects of α-synuclein posttranslational modifications. View Full-Text
Keywords: Synuclein; posttranslational modifications; synthesis Synuclein; posttranslational modifications; synthesis

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Pratt, M.R.; Abeywardana, T.; Marotta, N.P. Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications. Biomolecules 2015, 5, 1210-1227.

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