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A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules
A 24-amino acid leader peptide of a new human recombinant manganese superoxide dismutase can enter cells and carry molecules. Here, we demonstrated that six of the 24 amino acids penetrate cells through a particular gate represented by a specific amino acid sequence of the oestrogen receptor (ER). W...
Autores principales: | , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4698655/ https://www.ncbi.nlm.nih.gov/pubmed/26725847 http://dx.doi.org/10.1038/srep18691 |
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author | Borrelli, Antonella Schiattarella, Antonietta Mancini, Roberto Pica, Alessandra Pollio, Maria Laura Ruggiero, Maria Grazia Bonelli, Patrizia De Luca, Viviana Tuccillo, Franca Maria Capasso, Clemente Gori, Enrico Sanseverino, Marina Carpentieri, Andrea Birolo, Leila Pucci, Piero Rommelaere, Jean Mancini, Aldo |
author_facet | Borrelli, Antonella Schiattarella, Antonietta Mancini, Roberto Pica, Alessandra Pollio, Maria Laura Ruggiero, Maria Grazia Bonelli, Patrizia De Luca, Viviana Tuccillo, Franca Maria Capasso, Clemente Gori, Enrico Sanseverino, Marina Carpentieri, Andrea Birolo, Leila Pucci, Piero Rommelaere, Jean Mancini, Aldo |
author_sort | Borrelli, Antonella |
collection | PubMed |
description | A 24-amino acid leader peptide of a new human recombinant manganese superoxide dismutase can enter cells and carry molecules. Here, we demonstrated that six of the 24 amino acids penetrate cells through a particular gate represented by a specific amino acid sequence of the oestrogen receptor (ER). We analysed the internalization of the synthetic hexapeptide and the cytotoxic activity of the hexapeptide conjugated to cisplatin on a cell line panel. In most cell lines, the hexapeptide delivered an amount of cisplatin that was 2 to 8 times greater than that released by cisplatin when the drug was used alone. This increased delivery increases the therapeutic index of cisplatin and reduces side effects caused by a high dosage or long-term treatment times. We may consider this hexapeptide a new molecular carrier to deliver molecules with therapeutic activity into ER(+) cells for diagnostic purposes and clinical or immune therapy. |
format | Online Article Text |
id | pubmed-4698655 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-46986552016-01-13 A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules Borrelli, Antonella Schiattarella, Antonietta Mancini, Roberto Pica, Alessandra Pollio, Maria Laura Ruggiero, Maria Grazia Bonelli, Patrizia De Luca, Viviana Tuccillo, Franca Maria Capasso, Clemente Gori, Enrico Sanseverino, Marina Carpentieri, Andrea Birolo, Leila Pucci, Piero Rommelaere, Jean Mancini, Aldo Sci Rep Article A 24-amino acid leader peptide of a new human recombinant manganese superoxide dismutase can enter cells and carry molecules. Here, we demonstrated that six of the 24 amino acids penetrate cells through a particular gate represented by a specific amino acid sequence of the oestrogen receptor (ER). We analysed the internalization of the synthetic hexapeptide and the cytotoxic activity of the hexapeptide conjugated to cisplatin on a cell line panel. In most cell lines, the hexapeptide delivered an amount of cisplatin that was 2 to 8 times greater than that released by cisplatin when the drug was used alone. This increased delivery increases the therapeutic index of cisplatin and reduces side effects caused by a high dosage or long-term treatment times. We may consider this hexapeptide a new molecular carrier to deliver molecules with therapeutic activity into ER(+) cells for diagnostic purposes and clinical or immune therapy. Nature Publishing Group 2016-01-04 /pmc/articles/PMC4698655/ /pubmed/26725847 http://dx.doi.org/10.1038/srep18691 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Borrelli, Antonella Schiattarella, Antonietta Mancini, Roberto Pica, Alessandra Pollio, Maria Laura Ruggiero, Maria Grazia Bonelli, Patrizia De Luca, Viviana Tuccillo, Franca Maria Capasso, Clemente Gori, Enrico Sanseverino, Marina Carpentieri, Andrea Birolo, Leila Pucci, Piero Rommelaere, Jean Mancini, Aldo A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules |
title | A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules |
title_full | A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules |
title_fullStr | A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules |
title_full_unstemmed | A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules |
title_short | A new hexapeptide from the leader peptide of rMnSOD enters cells through the oestrogen receptor to deliver therapeutic molecules |
title_sort | new hexapeptide from the leader peptide of rmnsod enters cells through the oestrogen receptor to deliver therapeutic molecules |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4698655/ https://www.ncbi.nlm.nih.gov/pubmed/26725847 http://dx.doi.org/10.1038/srep18691 |
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