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Dianthin and Its Potential in Targeted Tumor Therapies

Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety. Dianthin-30 is very similar to saporin-S3 and saporin-S6, two RIPs often used to design targeted toxins for tumor therapy and already teste...

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Autor principal: Fuchs, Hendrik
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6832487/
https://www.ncbi.nlm.nih.gov/pubmed/31614697
http://dx.doi.org/10.3390/toxins11100592
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author Fuchs, Hendrik
author_facet Fuchs, Hendrik
author_sort Fuchs, Hendrik
collection PubMed
description Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety. Dianthin-30 is very similar to saporin-S3 and saporin-S6, two RIPs often used to design targeted toxins for tumor therapy and already tested in some clinical trials. Nevertheless, dianthin enzymes also exhibit differences to saporin with regard to structure, efficacy, toxicity, immunogenicity and production by heterologous expression. Some of the distinctions might make dianthin more suitable for targeted tumor therapies than other RIPs. The present review provides an overview of the history of dianthin discovery and illuminates its structure, function and role in targeted toxins. It further discusses the option to increase the efficacy of dianthin by endosomal escape enhancers.
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spelling pubmed-68324872019-11-25 Dianthin and Its Potential in Targeted Tumor Therapies Fuchs, Hendrik Toxins (Basel) Review Dianthin enzymes belong to ribosome-inactivating proteins (RIPs) of type 1, i.e., they only consist of a catalytic domain and do not have a cell binding moiety. Dianthin-30 is very similar to saporin-S3 and saporin-S6, two RIPs often used to design targeted toxins for tumor therapy and already tested in some clinical trials. Nevertheless, dianthin enzymes also exhibit differences to saporin with regard to structure, efficacy, toxicity, immunogenicity and production by heterologous expression. Some of the distinctions might make dianthin more suitable for targeted tumor therapies than other RIPs. The present review provides an overview of the history of dianthin discovery and illuminates its structure, function and role in targeted toxins. It further discusses the option to increase the efficacy of dianthin by endosomal escape enhancers. MDPI 2019-10-11 /pmc/articles/PMC6832487/ /pubmed/31614697 http://dx.doi.org/10.3390/toxins11100592 Text en © 2019 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Fuchs, Hendrik
Dianthin and Its Potential in Targeted Tumor Therapies
title Dianthin and Its Potential in Targeted Tumor Therapies
title_full Dianthin and Its Potential in Targeted Tumor Therapies
title_fullStr Dianthin and Its Potential in Targeted Tumor Therapies
title_full_unstemmed Dianthin and Its Potential in Targeted Tumor Therapies
title_short Dianthin and Its Potential in Targeted Tumor Therapies
title_sort dianthin and its potential in targeted tumor therapies
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6832487/
https://www.ncbi.nlm.nih.gov/pubmed/31614697
http://dx.doi.org/10.3390/toxins11100592
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