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

Biomolecules

Matthew R. Pratt¹  Tharindumala Abeywardana¹  Nicholas P. Marotta¹ 

[1] Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA; E-Mails:

关键词: Synuclein;    posttranslational modifications;    synthesis;   

DOI  :  10.3390/biom5031210

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.