Metal-Dependent DNA Recognition and Cell Internalization of Designed, Basic Peptides
Por favor, use este identificador para citas ou ligazóns a este ítem:
http://hdl.handle.net/10347/18335
Ficheiros no ítem
Metadatos do ítem
Título: | Metal-Dependent DNA Recognition and Cell Internalization of Designed, Basic Peptides |
Autor/a: | Learte Aymamí, Soraya Curado, Natalia Rodríguez Villar, Jéssica Vázquez Sentís, Marco Eugenio Mascareñas Cid, José Luis |
Centro/Departamento: | Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares Universidade de Santiago de Compostela. Departamento de Química Orgánica |
Data: | 2017 |
Editor: | American Chemical Society |
Cita bibliográfica: | Learte-Aymamí, S., Curado, N., Rodríguez, J., Vázquez, M., & Mascareñas, J. (2017). Metal-Dependent DNA Recognition and Cell Internalization of Designed, Basic Peptides. Journal Of The American Chemical Society, 139(45), 16188-16193. doi: 10.1021/jacs.7b07422 |
Resumo: | A fragment of the DNA basic region (br) of the GCN4 bZIP transcription factor has been modified to include two His residues at designed i and i+4 positions of its N-terminus. The resulting monomeric peptide (brHis2) does not bind to its consensus target DNA site (5′-GTCAT-3′). However, addition of Pd(en)Cl2 (en, ethylenediamine) promotes a high-affinity interaction with exquisite selectivity for this sequence. The peptide–DNA complex is disassembled by addition of a slight excess of a palladium chelator, and the interaction can be reversibly switched multiple times by playing with controlled amounts of either the metal complex or the chelator. Importantly, while the peptide brHis2 fails to translocate across cell membranes on its own, addition of the palladium reagent induces an efficient cell internalization of this peptide. In short, we report (1) a designed, short peptide that displays highly selective, major groove DNA binding, (2) a reversible, metal-dependent DNA interaction, and (3) a metal-promoted cell internalization of this basic peptide |
Versión do editor: | https://doi.org/10.1021/jacs.7b07422 |
URI: | http://hdl.handle.net/10347/18335 |
DOI: | 10.1021/jacs.7b07422 |
ISSN: | 0002-7863 |
E-ISSN: | 1520-5126 |
Dereitos: | © 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (https://pubs.acs.org/page/policy/authorchoice_termsofuse.html), which permits copying and redistribution of the article or any adaptations for non-commercial purposes |
Coleccións
-
- CIQUS-Artigos [475]
- QO-Artigos [436]
A licenza do ítem descríbese como
© 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (https://pubs.acs.org/page/policy/authorchoice_termsofuse.html), which permits copying and redistribution of the article or any adaptations for non-commercial purposes
© 2017 American Chemical Society This is an open access article published under an ACS AuthorChoice License (https://pubs.acs.org/page/policy/authorchoice_termsofuse.html), which permits copying and redistribution of the article or any adaptations for non-commercial purposes