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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...

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Detalles Bibliográficos
Autores principales: Pratt, Matthew R., Abeywardana, Tharindumala, Marotta, Nicholas P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
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.
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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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