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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MDPI AG
2015-06-01
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Series: | Biomolecules |
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Online Access: | http://www.mdpi.com/2218-273X/5/3/1210 |
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author | Matthew R. Pratt Tharindumala Abeywardana Nicholas P. Marotta |
author_facet | Matthew R. Pratt Tharindumala Abeywardana Nicholas P. Marotta |
author_sort | Matthew R. Pratt |
collection | DOAJ |
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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id | doaj.art-31959b78c6de42eb9d845db3f687c2b6 |
institution | Directory Open Access Journal |
issn | 2218-273X |
language | English |
last_indexed | 2024-12-22T19:13:39Z |
publishDate | 2015-06-01 |
publisher | MDPI AG |
record_format | Article |
series | Biomolecules |
spelling | doaj.art-31959b78c6de42eb9d845db3f687c2b62022-12-21T18:15:36ZengMDPI AGBiomolecules2218-273X2015-06-01531210122710.3390/biom5031210biom5031210Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational ModificationsMatthew R. Pratt0Tharindumala Abeywardana1Nicholas P. Marotta2Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USADepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USADepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USAα-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.http://www.mdpi.com/2218-273X/5/3/1210Synucleinposttranslational modificationssynthesis |
spellingShingle | Matthew R. Pratt Tharindumala Abeywardana Nicholas P. Marotta Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications Biomolecules Synuclein posttranslational modifications synthesis |
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 | Synuclein posttranslational modifications synthesis |
url | http://www.mdpi.com/2218-273X/5/3/1210 |
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