Stereoselective self-assembly of DNA binding helicates directed by the Viral β-Annulus Trimeric Peptide Motif
| dc.contributor.affiliation | Universidade de Santiago de Compostela. Centro de Investigación en Química Biolóxica e Materiais Moleculares | gl |
| dc.contributor.affiliation | Universidade de Santiago de Compostela. Departamento de Química Inorgánica | gl |
| dc.contributor.affiliation | Universidade de Santiago de Compostela. Departamento de Química Orgánica | gl |
| dc.contributor.author | Gómez González, Jacobo | |
| dc.contributor.author | Bouzada Reboredo, David | |
| dc.contributor.author | Pérez Márquez, Lidia Ana | |
| dc.contributor.author | Sciortino, Giuseppe | |
| dc.contributor.author | Maréchal, Jean-Didier | |
| dc.contributor.author | Vázquez López, Miguel | |
| dc.contributor.author | Vázquez Sentis, Marco Eugenio | |
| dc.date.accessioned | 2022-08-09T08:18:28Z | |
| dc.date.available | 2022-08-09T08:18:28Z | |
| dc.date.issued | 2021 | |
| dc.description.abstract | 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 | gl |
| dc.description.peerreviewed | SI | gl |
| dc.description.sponsorship | Financial support from the Spanish grant RTI2018-099877-B-I00, the Xunta de Galicia (Centro singular de Investigación de Galicia accreditation 2016–2019, ED431G/09, and ED431B 2018/04), and the European Union (European Regional Development Fund - ERDF) is gratefully acknowledged. J.G.-G. thanks the Spanish MINECO for his FPI fellowship. D.B. thanks the CIQUS for his 2018 PhD fellowship. G.S. and J.-D.M. thank Spanish MINECO (grant CTQ2017-87889-P) and Generalitat de Catalunya (2017SGR1323) for the financial support. Finally, we would like to thank Prof. Kazunori Matsuura at Tottori University for his valuable input during the preparation of this manuscript | gl |
| dc.identifier.citation | Bioconjugate Chem. 2021, 32, 1564−1569. https://doi.org/10.1021/acs.bioconjchem.1c00312 | gl |
| dc.identifier.doi | 10.1021/acs.bioconjchem.1c00312 | |
| dc.identifier.issn | 1043-1802 | |
| dc.identifier.uri | http://hdl.handle.net/10347/29039 | |
| dc.language.iso | eng | gl |
| dc.publisher | ACS Publications | gl |
| dc.relation.projectID | info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/RTI2018-099877-B-I00/ES/PLATAFORMAS PEPTIDICAS PARA APLICACIONES EN QUIMICA (BIO)SUPRAMOLECULAR Y DE MATERIALES, CATALISIS Y SENSORES (SWISSKNIFE) | gl |
| dc.relation.projectID | info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2017-2020/CTQ2017-87889-P/ES/DE LA CATALISIS MOLECULAR A LA SUPRA-BIO-CATALISIS, UN ENFOQUE COMPUTACIONAL | gl |
| dc.relation.publisherversion | https://doi.org/10.1021/acs.bioconjchem.1c00312 | gl |
| dc.rights | © 2021 American Chemical Society. This work is licenced under a Creative Commons Attribution 4.0 International licence (https://creativecommons.org/licenses/by/4.0/legalcode) Atribución 4.0 Internacional | gl |
| dc.rights.accessRights | open access | gl |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | |
| dc.subject | Genetics | gl |
| dc.subject | Ligands | gl |
| dc.subject | Monomers | gl |
| dc.subject | Peptides and proteins | gl |
| dc.subject | Supramolecular structures and assemblies | gl |
| dc.title | Stereoselective self-assembly of DNA binding helicates directed by the Viral β-Annulus Trimeric Peptide Motif | gl |
| dc.type | journal article | gl |
| dc.type.hasVersion | VoR | gl |
| dspace.entity.type | Publication | |
| relation.isAuthorOfPublication | 811a1eac-4048-4ed9-a56f-c1104cc20827 | |
| relation.isAuthorOfPublication | 49ee56a2-7094-407b-8108-b55c5968f241 | |
| relation.isAuthorOfPublication.latestForDiscovery | 811a1eac-4048-4ed9-a56f-c1104cc20827 |
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