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Stereoselective Self-Assembly of DNA Binding Helicates Directed by the Viral β-Annulus Trimeric Peptide Motif
[Image: see text] Combining coordination chemistry and peptide engineering offers extraordinary opportunities for developing novel molecular (supra)structures. Here, we demonstrate that the β-annulus motif is capable of directing the stereoselective assembly of designed peptides containing 2,2′-bipy...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8485332/ https://www.ncbi.nlm.nih.gov/pubmed/34320309 http://dx.doi.org/10.1021/acs.bioconjchem.1c00312 |
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author | Gómez-González, Jacobo Bouzada, David Pérez-Márquez, Lidia A. Sciortino, Giuseppe Maréchal, Jean-Didier Vázquez López, Miguel Vázquez, M. Eugenio |
author_facet | Gómez-González, Jacobo Bouzada, David Pérez-Márquez, Lidia A. Sciortino, Giuseppe Maréchal, Jean-Didier Vázquez López, Miguel Vázquez, M. Eugenio |
author_sort | Gómez-González, Jacobo |
collection | PubMed |
description | [Image: see text] Combining coordination chemistry and peptide engineering offers extraordinary opportunities for developing novel molecular (supra)structures. Here, we demonstrate that the β-annulus motif is capable of directing the stereoselective assembly of designed peptides containing 2,2′-bipyridine ligands into parallel three-stranded chiral peptide helicates, and that these helicates selectively bind with high affinity to three-way DNA junctions. |
format | Online Article Text |
id | pubmed-8485332 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-84853322021-10-01 Stereoselective Self-Assembly of DNA Binding Helicates Directed by the Viral β-Annulus Trimeric Peptide Motif Gómez-González, Jacobo Bouzada, David Pérez-Márquez, Lidia A. Sciortino, Giuseppe Maréchal, Jean-Didier Vázquez López, Miguel Vázquez, M. Eugenio Bioconjug Chem [Image: see text] Combining coordination chemistry and peptide engineering offers extraordinary opportunities for developing novel molecular (supra)structures. Here, we demonstrate that the β-annulus motif is capable of directing the stereoselective assembly of designed peptides containing 2,2′-bipyridine ligands into parallel three-stranded chiral peptide helicates, and that these helicates selectively bind with high affinity to three-way DNA junctions. American Chemical Society 2021-07-28 2021-08-18 /pmc/articles/PMC8485332/ /pubmed/34320309 http://dx.doi.org/10.1021/acs.bioconjchem.1c00312 Text en © 2021 American Chemical Society https://creativecommons.org/licenses/by/4.0/Permits the broadest form of re-use including for commercial purposes, provided that author attribution and integrity are maintained (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Gómez-González, Jacobo Bouzada, David Pérez-Márquez, Lidia A. Sciortino, Giuseppe Maréchal, Jean-Didier Vázquez López, Miguel Vázquez, M. Eugenio Stereoselective Self-Assembly of DNA Binding Helicates Directed by the Viral β-Annulus Trimeric Peptide Motif |
title | Stereoselective Self-Assembly
of DNA Binding Helicates
Directed by the Viral β-Annulus Trimeric Peptide Motif |
title_full | Stereoselective Self-Assembly
of DNA Binding Helicates
Directed by the Viral β-Annulus Trimeric Peptide Motif |
title_fullStr | Stereoselective Self-Assembly
of DNA Binding Helicates
Directed by the Viral β-Annulus Trimeric Peptide Motif |
title_full_unstemmed | Stereoselective Self-Assembly
of DNA Binding Helicates
Directed by the Viral β-Annulus Trimeric Peptide Motif |
title_short | Stereoselective Self-Assembly
of DNA Binding Helicates
Directed by the Viral β-Annulus Trimeric Peptide Motif |
title_sort | stereoselective self-assembly
of dna binding helicates
directed by the viral β-annulus trimeric peptide motif |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8485332/ https://www.ncbi.nlm.nih.gov/pubmed/34320309 http://dx.doi.org/10.1021/acs.bioconjchem.1c00312 |
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