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

Matthew R. Pratt; Tharindumala Abeywardana; Nicholas P. Marotta

doi:10.3390/biom5031210

Biomolecules (Jun 2015)

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

Matthew R. Pratt,
Tharindumala Abeywardana,
Nicholas P. Marotta

Affiliations

Matthew R. Pratt: Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA
Tharindumala Abeywardana: Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA
Nicholas P. Marotta: Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA

DOI: https://doi.org/10.3390/biom5031210
Journal volume & issue: Vol. 5, no. 3
pp. 1210 – 1227

Abstract

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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.

Published in Biomolecules

ISSN: 2218-273X (Online)
Publisher: MDPI AG
Country of publisher: Switzerland
LCC subjects: Science: Microbiology
Website: https://www.mdpi.com/journal/biomolecules

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