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Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications
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...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4598748/ https://www.ncbi.nlm.nih.gov/pubmed/26120904 http://dx.doi.org/10.3390/biom5031210 |
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author | Pratt, Matthew R. Abeywardana, Tharindumala Marotta, Nicholas P. |
author_facet | Pratt, Matthew R. Abeywardana, Tharindumala Marotta, Nicholas P. |
author_sort | Pratt, Matthew R. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4598748 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-45987482015-10-15 Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications Pratt, Matthew R. Abeywardana, Tharindumala Marotta, Nicholas P. Biomolecules Review 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. MDPI 2015-06-25 /pmc/articles/PMC4598748/ /pubmed/26120904 http://dx.doi.org/10.3390/biom5031210 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Pratt, Matthew R. Abeywardana, Tharindumala Marotta, Nicholas P. Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications |
title | Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications |
title_full | Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications |
title_fullStr | Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications |
title_full_unstemmed | Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications |
title_short | Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications |
title_sort | synthetic proteins and peptides for the direct interrogation of α-synuclein posttranslational modifications |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4598748/ https://www.ncbi.nlm.nih.gov/pubmed/26120904 http://dx.doi.org/10.3390/biom5031210 |
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