Conformational conversion during controlled oligomerization into nonamylogenic protein nanoparticles
Sanchez, Julieta M. (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Sánchez-García, Laura (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Pesarrodona Roches, Mireia (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Serna, Naroa (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Sánchez Chardi, Alejandro (Universitat Autònoma de Barcelona. Servei de Microscòpia)
Unzueta Elorza, Ugutz (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Mangues, Ramon 1957- (Institut Germans Trias i Pujol. Institut de Recerca contra la Leucèmia Josep Carreras)
Vázquez Gómez, Esther (Universitat Autònoma de Barcelona. Departament de Genètica i de Microbiologia)
Villaverde Corrales, Antonio (Universitat Autònoma de Barcelona. Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Fecha:	2018
Resumen:	Protein materials are rapidly gaining interest in materials sciences and nanomedicine because of their intrinsic biocompatibility and full biodegradability. The controlled construction of supramolecular entities relies on the controlled oligomerization of individual polypeptides, achievable through different strategies. Because of the potential toxicity of amyloids, those based on alternative molecular organizations are particularly appealing, but the structural bases on nonamylogenic oligomerization remain poorly studied. We have applied spectrofluorimetry and spectropolarimetry to identify the conformational conversion during the oligomerization of His-tagged cationic stretches into regular nanoparticles ranging around 11 nm, useful for tumor-targeted drug delivery. We demonstrate that the novel conformation acquired by the proteins, as building blocks of these supramolecular assemblies, shows different extents of compactness and results in a beta structure enrichment that enhances their structural stability. The conformational profiling presented here offers clear clues for understanding and tailoring the process of nanoparticle formation through the use of cationic and histidine rich stretches in the context of protein materials usable in advanced nanomedical strategies.
Ayudas:	Ministerio de Ciencia e Innovación BIO2016-76063-R Instituto de Salud Carlos III PI15/00378 Instituto de Salud Carlos III PIE15/00028 Instituto de Salud Carlos III PI15/00272 Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/FI_B100063 Agència de Gestió d'Ajuts Universitaris i de Recerca 2017/SGR-229
Nota:	Altres ajuts: protein production and DLS have been partially performed by the ICTS "NANBIOSIS", more specifically by the Protein Production Platform of CIBER-BBN/IBB (http://www. nanbiosis.es/unit/u1-protein-production-platform-ppp/) and the Biomaterial Processing and Nanostructuring Unit (http://www.nanbiosis.es/portfolio/u6-biomaterial-processing-and-nanostructuring-unit/). J.M.S. is a Career Investigator from CONICET (Government of Argentina), N.S. was supported by a predoctoral fellowship from the Government of Navarra, and U.U. received a Sara Borrell postdoctoral fellowship from AGAUR. A.V. received an ICREA ACADEMIA award. This study has been funded by CIBER-BBN (project VENOM4-CANCER) granted to A.V.
Derechos:	Tots els drets reservats.
Lengua:	Anglès
Documento:	Article ; recerca ; Versió acceptada per publicar
Materia:	Conformational conversion ; Molecular organization ; Nanoparticle formation ; Protein nanoparticles ; Spectropolarimetry ; Structural stabilities ; Supramolecular assemblies ; Tumor-targeted drug deliveries ; Antimicrobial Cationic Peptides ; Antineoplastic Agents ; Green Fluorescent Proteins ; Nanoparticles ; Protein Conformation, beta-Strand ; Protein Multimerization ; Protein Stability ; Recombinant Proteins
Publicado en:	Biomacromolecules, Vol. 19, issue 9 (Sep. 2018) , p. 3788-3797, ISSN 1526-4602

DOI: 10.1021/acs.biomac.8b00924
PMID: 30052033

Postprint 29 p, 849.9 KB

El registro aparece en las colecciones:
Documentos de investigación > Documentos de los grupos de investigación de la UAB > Centros y grupos de investigación (producción científica) > Ciencias de la salud y biociencias > Institut d'Investigació en Ciencies de la Salut Germans Trias i Pujol (IGTP) > Instituto de Investigación contra la Leucemia Josep Carreras
Documentos de investigación > Documentos de los grupos de investigación de la UAB > Centros y grupos de investigación (producción científica) > Ciencias de la salud y biociencias > Instituto de Biotecnología y de Biomedicina (IBB)
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