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Updated: Apr 8, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
Published on: May 30, 2015
Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications
Matthew R Pratt1,2, Tharindumala Abeywardana3, Nicholas P Marotta4
1Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. matthew.pratt@usc.edu.
Abstract:
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.
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