Mostrar el registro sencillo del ítem
dc.contributor.author
Voltà Durán, Eric
dc.contributor.author
Sanchez, Julieta Maria
dc.contributor.author
López Laguna, Hèctor
dc.contributor.author
Parladé, Eloi
dc.contributor.author
Sánchez García, Laura
dc.contributor.author
Sánchez Chardi, Alejandro
dc.contributor.author
de Marco, Ario
dc.contributor.author
Unzueta, Ugutz
dc.contributor.author
Vázquez, Esther
dc.contributor.author
Villaverde Corrales, Antonio
dc.date.available
2022-09-05T11:59:13Z
dc.date.issued
2022-06-17
dc.identifier.citation
Voltà Durán, Eric; Sanchez, Julieta Maria; López Laguna, Hèctor; Parladé, Eloi; Sánchez García, Laura; et al.; The spectrum of building block conformers sustains the biophysical properties of clinically-oriented self-assembling protein nanoparticles; Springer; Science China Materials; 65; 6; 17-6-2022; 1662-1670
dc.identifier.issn
2095-8226
dc.identifier.uri
http://hdl.handle.net/11336/167309
dc.description.abstract
Histidine-rich peptides confer self-assembling properties to recombinant proteins through the supramolecular coordination with divalent cations. This fact allows the cost-effective, large-scale generation of microscopic and macroscopic protein materials with intriguing biomedical properties. Among such materials, resulting from the simple bioproduction of protein building blocks, homomeric nanoparticles are of special value as multivalent interactors and drug carriers. Interestingly, we have here identified that the assembly of a given His-tagged protein might render distinguishable categories of self-assembling protein nanoparticles. This fact has been scrutinized through the nanobody-containing fusion proteins EM1-GFP-H6 and A3C8-GFP-H6, whose biosynthesis results in two distinguishable populations of building blocks. In one of them, the assembling and disassembling is controllable by cations. However, a second population immediately self-assembles upon purification through a non-regulatable pathway, rendering larger nanoparticles with specific biological properties. The structural analyses of both model proteins and nanoparticles revealed important conformational variability in the building blocks. This fact renders different structural and functional categories of the final soft materials resulting from the participation of energetically unstable intermediates in the oligomerization process. These data illustrate the complexity of the Hismediated protein assembling in recombinant proteins but they also offer clues for a better design and refinement of protein-based nanomedicines, which, resulting from biological fabrication, show an architectonic flexibility unusual among biomaterials.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Springer
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
RECOMBINANT PROTEINS
dc.subject
SELF-ASSEMBLING
dc.subject
PROTEIN MATERIALS
dc.subject
NANOPARTICLES
dc.subject
BIOMATERIALS
dc.subject.classification
Nano-materiales
dc.subject.classification
Nanotecnología
dc.subject.classification
INGENIERÍAS Y TECNOLOGÍAS
dc.title
The spectrum of building block conformers sustains the biophysical properties of clinically-oriented self-assembling protein nanoparticles
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-07-04T19:31:05Z
dc.identifier.eissn
2199-4501
dc.journal.volume
65
dc.journal.number
6
dc.journal.pagination
1662-1670
dc.journal.pais
Suiza
dc.journal.ciudad
Cham
dc.description.fil
Fil: Voltà Durán, Eric. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
dc.description.fil
Fil: Sanchez, Julieta Maria. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigaciones Biológicas y Tecnológicas. Universidad Nacional de Córdoba. Facultad de Ciencias Exactas, Físicas y Naturales. Instituto de Investigaciones Biológicas y Tecnológicas; Argentina. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
dc.description.fil
Fil: López Laguna, Hèctor. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
dc.description.fil
Fil: Parladé, Eloi. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
dc.description.fil
Fil: Sánchez García, Laura. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España. Universitat Internacional de Catalunya; España
dc.description.fil
Fil: Sánchez Chardi, Alejandro. Universitat Autònoma de Barcelona; España. Universidad de Barcelona; España
dc.description.fil
Fil: de Marco, Ario. University of Nova Gorica; Eslovenia
dc.description.fil
Fil: Unzueta, Ugutz. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España. Biomedical Research Institute Sant Pau; España
dc.description.fil
Fil: Vázquez, Esther. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
dc.description.fil
Fil: Villaverde Corrales, Antonio. Universitat Autònoma de Barcelona; España. Centro de Investigación Biomédica en Red de Bioingeniería, Biomateriales y Nanomedicina; España
dc.journal.title
Science China Materials
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1007/s40843-021-1914-0
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://link.springer.com/article/10.1007/s40843-021-1914-0
Archivos asociados