Biofabrication of functional protein nanoparticles through simple His-tag engineering

We have developed a simple, robust, and fully transversal approach for the a-la-carte fabrication of functional multimeric nanoparticles with potential biomedical applications, validated here by a set of diverse and unrelated polypeptides. The proposed concept is based on the controlled coordination...

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Detalles Bibliográficos
Autores: Lopez-Laguna, H, Sanchez, JM, Carratala, JV, Rojas-Pena, M, Sanchez-Garcia, L, Parlade, E, Sanchez-Chardi, A, Volta-Duran, E, Serna, N, Cano-Garrido, O, Flores, S, Ferrer-Miralles, N, Nolan, V, de Marco, A, Roher, N, Unzueta, U, Vazquez, E, Villaverde, A
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2021
País:España
Institución:Institut d’Investigació Biomèdica Sant Pau (IIB Sant Pau)
Repositorio:r-IIB SANT PAU. Repositorio Institucional de Producción Científica del Instituto de Investigación Biomédica Sant Pau
OAI Identifier:oai:iibsantpau.fundanetsuite.com:p4335
Acceso en línea:https://iibsantpau.fundanetsuite.com/Publicaciones/ProdCientif/PublicacionFrw.aspx?id=4335
https://europepmc.org/articles/pmc8483566?pdf=render
Access Level:acceso abierto
Palabra clave:Nanoparticles
Protein engineering
Divalent cations
Protein materials
Biomaterials design
Descripción
Sumario:We have developed a simple, robust, and fully transversal approach for the a-la-carte fabrication of functional multimeric nanoparticles with potential biomedical applications, validated here by a set of diverse and unrelated polypeptides. The proposed concept is based on the controlled coordination between Zn2+ ions and His residues in His-tagged proteins. This approach results in a spontaneous and reproducible protein assembly as nanoscale oligomers that keep the original functionalities of the protein building blocks. The assembly of these materials is not linked to particular polypeptide features, and it is based on an environmentally friendly and sustainable approach. The resulting nanoparticles, with dimensions ranging between 10 and 15 nm, are regular in size, are architecturally stable, are fully functional, and serve as intermediates in a more complex assembly process, resulting in the formation of microscale protein materials. Since most of the recombinant proteins produced by biochemical and biotechnological industries and intended for biomedical research are His-tagged, the green biofabrication procedure proposed here can be straightforwardly applied to a huge spectrum of protein species for their conversion into their respective nanostructured formats.