Biomolecules | |
Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications | |
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.
【 预 览 】
Files | Size | Format | View |
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RO202003190010959ZK.pdf | 3205KB | download |