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Versatile synthesis of the signaling peptide glorin
We present a versatile synthesis of the eukaryotic signaling peptide glorin as well as glorinamide, a synthetic analog. The ability of these compounds to activate glorin-induced genes in the social amoeba Polysphondylium pallidum was evaluated by quantitative reverse transcription PCR, whereby both...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Beilstein-Institut
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5331329/ https://www.ncbi.nlm.nih.gov/pubmed/28326133 http://dx.doi.org/10.3762/bjoc.13.27 |
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author | Barnett, Robert Raszkowski, Daniel Winckler, Thomas Stallforth, Pierre |
author_facet | Barnett, Robert Raszkowski, Daniel Winckler, Thomas Stallforth, Pierre |
author_sort | Barnett, Robert |
collection | PubMed |
description | We present a versatile synthesis of the eukaryotic signaling peptide glorin as well as glorinamide, a synthetic analog. The ability of these compounds to activate glorin-induced genes in the social amoeba Polysphondylium pallidum was evaluated by quantitative reverse transcription PCR, whereby both compounds showed bioactivity comparable to a glorin standard. This synthetic route will be useful in conducting detailed structure–activity relationship studies as well as in the design of chemical probes to dissect glorin-mediated signaling pathways. |
format | Online Article Text |
id | pubmed-5331329 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Beilstein-Institut |
record_format | MEDLINE/PubMed |
spelling | pubmed-53313292017-03-21 Versatile synthesis of the signaling peptide glorin Barnett, Robert Raszkowski, Daniel Winckler, Thomas Stallforth, Pierre Beilstein J Org Chem Full Research Paper We present a versatile synthesis of the eukaryotic signaling peptide glorin as well as glorinamide, a synthetic analog. The ability of these compounds to activate glorin-induced genes in the social amoeba Polysphondylium pallidum was evaluated by quantitative reverse transcription PCR, whereby both compounds showed bioactivity comparable to a glorin standard. This synthetic route will be useful in conducting detailed structure–activity relationship studies as well as in the design of chemical probes to dissect glorin-mediated signaling pathways. Beilstein-Institut 2017-02-08 /pmc/articles/PMC5331329/ /pubmed/28326133 http://dx.doi.org/10.3762/bjoc.13.27 Text en Copyright © 2017, Barnett et al. https://creativecommons.org/licenses/by/4.0https://www.beilstein-journals.org/bjoc/termsThis is an Open Access article under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. The license is subject to the Beilstein Journal of Organic Chemistry terms and conditions: (https://www.beilstein-journals.org/bjoc/terms) |
spellingShingle | Full Research Paper Barnett, Robert Raszkowski, Daniel Winckler, Thomas Stallforth, Pierre Versatile synthesis of the signaling peptide glorin |
title | Versatile synthesis of the signaling peptide glorin |
title_full | Versatile synthesis of the signaling peptide glorin |
title_fullStr | Versatile synthesis of the signaling peptide glorin |
title_full_unstemmed | Versatile synthesis of the signaling peptide glorin |
title_short | Versatile synthesis of the signaling peptide glorin |
title_sort | versatile synthesis of the signaling peptide glorin |
topic | Full Research Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5331329/ https://www.ncbi.nlm.nih.gov/pubmed/28326133 http://dx.doi.org/10.3762/bjoc.13.27 |
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