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Development of a Photoactivatable Protein Phosphatase-1-Disrupting Peptide
[Image: see text] We describe here the development of a photoreleasable version of a protein phosphatase-1 (PP1)-disrupting peptide (PDP-Nal) that triggers protein phosphatase-1 activity. PDP-Nal is a 23 mer that binds to PP1 through several interactions. It was photocaged on a tyrosine residue, whi...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2019
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7011174/ https://www.ncbi.nlm.nih.gov/pubmed/31841001 http://dx.doi.org/10.1021/acs.joc.9b02548 |
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author | Trebacz, Malgorzata Wang, Yansong Makotta, Leslie Henschke, Lars Köhn, Maja |
author_facet | Trebacz, Malgorzata Wang, Yansong Makotta, Leslie Henschke, Lars Köhn, Maja |
author_sort | Trebacz, Malgorzata |
collection | PubMed |
description | [Image: see text] We describe here the development of a photoreleasable version of a protein phosphatase-1 (PP1)-disrupting peptide (PDP-Nal) that triggers protein phosphatase-1 activity. PDP-Nal is a 23 mer that binds to PP1 through several interactions. It was photocaged on a tyrosine residue, which required the exchange of phenylalanine in PDP-Nal to tyrosine in order to disrupt the most important binding interface. This PDP-caged can be light-controlled in live cells. |
format | Online Article Text |
id | pubmed-7011174 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-70111742020-02-12 Development of a Photoactivatable Protein Phosphatase-1-Disrupting Peptide Trebacz, Malgorzata Wang, Yansong Makotta, Leslie Henschke, Lars Köhn, Maja J Org Chem [Image: see text] We describe here the development of a photoreleasable version of a protein phosphatase-1 (PP1)-disrupting peptide (PDP-Nal) that triggers protein phosphatase-1 activity. PDP-Nal is a 23 mer that binds to PP1 through several interactions. It was photocaged on a tyrosine residue, which required the exchange of phenylalanine in PDP-Nal to tyrosine in order to disrupt the most important binding interface. This PDP-caged can be light-controlled in live cells. American Chemical Society 2019-12-16 2020-02-07 /pmc/articles/PMC7011174/ /pubmed/31841001 http://dx.doi.org/10.1021/acs.joc.9b02548 Text en Copyright © 2019 American Chemical Society This is an open access article published under a Creative Commons Non-Commercial No Derivative Works (CC-BY-NC-ND) Attribution License (http://pubs.acs.org/page/policy/authorchoice_ccbyncnd_termsofuse.html) , which permits copying and redistribution of the article, and creation of adaptations, all for non-commercial purposes. |
spellingShingle | Trebacz, Malgorzata Wang, Yansong Makotta, Leslie Henschke, Lars Köhn, Maja Development of a Photoactivatable Protein Phosphatase-1-Disrupting Peptide |
title | Development of a
Photoactivatable Protein Phosphatase-1-Disrupting
Peptide |
title_full | Development of a
Photoactivatable Protein Phosphatase-1-Disrupting
Peptide |
title_fullStr | Development of a
Photoactivatable Protein Phosphatase-1-Disrupting
Peptide |
title_full_unstemmed | Development of a
Photoactivatable Protein Phosphatase-1-Disrupting
Peptide |
title_short | Development of a
Photoactivatable Protein Phosphatase-1-Disrupting
Peptide |
title_sort | development of a
photoactivatable protein phosphatase-1-disrupting
peptide |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7011174/ https://www.ncbi.nlm.nih.gov/pubmed/31841001 http://dx.doi.org/10.1021/acs.joc.9b02548 |
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