Hybrid gold nanoparticle-quantum dot self-assembled nanostructures driven by complementary artificial proteins.


Journal

Nanoscale
ISSN: 2040-3372
Titre abrégé: Nanoscale
Pays: England
ID NLM: 101525249

Informations de publication

Date de publication:
20 Feb 2020
Historique:
pubmed: 12 2 2020
medline: 20 11 2020
entrez: 12 2 2020
Statut: ppublish

Résumé

Hybrid nanostructures are constructed by the direct coupling of fluorescent quantum dots and plasmonic gold nanoparticles. Self-assembly is directed by the strong affinity between two artificial α-repeat proteins that are introduced in the capping layers of the nanoparticles at a controlled surface density. The proteins have been engineered to exhibit a high mutual affinity, corresponding to a dissociation constant in the nanomolar range, towards the protein-functionalized quantum dots and gold nanoparticles. Protein-mediated self-assembly is evidenced by surface plasmon resonance and gel electrophoresis. The size and the structure of colloidal superstructures of complementary nanoparticles are analyzed by transmission electron microscopy and small angle X-ray scattering. The size of the superstructures is determined by the number of proteins per nanoparticle. The well-defined geometry of the rigid protein complex sets a highly uniform interparticle distance of 8 nm that affects the emission properties of the quantum dots in the hybrid ensembles. Our results open the route to the design of hybrid emitter-plasmon colloidal assemblies with controlled near-field coupling and better optical response.

Identifiants

pubmed: 32043516
doi: 10.1039/c9nr09987e
doi:

Substances chimiques

Proteins 0
Gold 7440-57-5

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

4612-4621

Auteurs

Maxence Fernandez (M)

University Rennes 1, Institute of Chemical Sciences, UMR 6226 CNRS, Campus Beaulieu, F-35042 Rennes, France. valerie.marchi@univ-rennes1.fr.

Agathe Urvoas (A)

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France.

Pascale Even-Hernandez (P)

University Rennes 1, Institute of Chemical Sciences, UMR 6226 CNRS, Campus Beaulieu, F-35042 Rennes, France. valerie.marchi@univ-rennes1.fr.

Agnès Burel (A)

University Rennes 1, Microscopy Rennes Imaging Center, UMS3480 BIOSIT, Campus Villejean, Rennes, France.

Cristelle Mériadec (C)

University Rennes 1, Institut de Physique de Rennes, UMR 6251 CNRS, Campus Beaulieu, F-35042 Rennes, France.

Franck Artzner (F)

University Rennes 1, Institut de Physique de Rennes, UMR 6251 CNRS, Campus Beaulieu, F-35042 Rennes, France.

Tahar Bouceba (T)

Sorbonne Université, CNRS, Institut de Biologie Paris-Seine (IBPS), Protein engineering platform, Molecular Interaction Service, F-75005 Paris, France.

Philippe Minard (P)

Institute for Integrative Biology of the Cell (I2BC), CEA, CNRS, Univ. Paris-Sud, Université Paris-Saclay, 91198 Gif-sur-Yvette Cedex, France.

Erik Dujardin (E)

Groupe NanoSciences-CEMES, CNRS UPR 8011, 29 rue J. Marvig, B.P. 94347, F-31055 Toulouse, France.

Valérie Marchi (V)

University Rennes 1, Institute of Chemical Sciences, UMR 6226 CNRS, Campus Beaulieu, F-35042 Rennes, France. valerie.marchi@univ-rennes1.fr.

Articles similaires

Databases, Protein Protein Domains Protein Folding Proteins Deep Learning
Humans Hyaluronic Acid Osteoarthritis, Hip Female Middle Aged
Cobalt Azo Compounds Ferric Compounds Polyesters Photolysis
Humans Computational Biology ROC Curve Algorithms Proteins

Classifications MeSH