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

Biomolecules. 2015 Jun 25;5(3):1210-27. doi: 10.3390/biom5031210.

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.

Keywords: Synuclein; posttranslational modifications; synthesis.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Chemistry Techniques, Synthetic
  • Humans
  • Peptides / chemical synthesis
  • Peptides / pharmacology*
  • Protein Processing, Post-Translational / drug effects*
  • Proteins / chemical synthesis
  • Proteins / pharmacology*
  • alpha-Synuclein / chemistry
  • alpha-Synuclein / metabolism*

Substances

  • Peptides
  • Proteins
  • alpha-Synuclein