Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies

verfasst von: Olivia Cano-Garrido, Escarlata Rodríguez-Carmona, César Díez-Gil, Esther Vázquez, Elisa Elizondo, Rafael Cubarsi, Joaquin Seras-Franzoso, José Luis Corchero, Ursula Rinas, Imma Ratera, Nora Ventosa, Jaume Veciana, Antonio Villaverde, Elena García-Fruitós
Abstract: Slow protein release from amyloidal materials is a molecular platform used by nature to control protein hormone secretion in the endocrine system. The molecular mechanics of the sustained protein release from amyloids remains essentially unexplored. Inclusion bodies (IBs) are natural amyloids that occur as discrete protein nanoparticles in recombinant bacteria. These protein clusters have been recently explored as protein-based functional biomaterials with diverse biomedical applications, and adapted as nanopills to deliver recombinant protein drugs into mammalian cells. Interestingly, the slow protein release from IBs does not significantly affect the particulate organization and morphology of the material, suggesting the occurrence of a tight scaffold. Here, we have determined, by using a combined set of analytical approaches, a sponge-like supramolecular organization of IBs combining differently folded protein versions (amyloid and native-like), which supports both mechanical stability and sustained protein delivery. Apart from offering structural clues about how amyloid materials release their monomeric protein components, these findings open exciting possibilities for the tailored development of smart biofunctional materials, adapted to mimic the functions of amyloid-based secretory glands of higher organisms.
Organisationseinheit(en): Institut für Technische Chemie
Externe Organisation(en): Universidad Autónoma de Barcelona (UAB)
Centros de Investigacion Biomedica en Red - CIBER
Spanish National Research Council (CSIC)
Universitat Politècnica de Catalunya
Helmholtz-Zentrum für Infektionsforschung GmbH (HZI)
Typ: Artikel
Journal: Acta biomaterialia
Band: 9
Seiten: 6134-6142
Anzahl der Seiten: 9
ISSN: 1742-7061
Publikationsdatum: 04.2013
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Biotechnologie, Biomaterialien, Biochemie, Biomedizintechnik, Molekularbiologie
Elektronische Version(en): https://doi.org/10.1016/j.actbio.2012.11.033 (Zugang: Geschlossen)

BibTeX

@article{16a75e69eab44e63927461067eadcee9,
title = "Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies",
abstract = "Slow protein release from amyloidal materials is a molecular platform used by nature to control protein hormone secretion in the endocrine system. The molecular mechanics of the sustained protein release from amyloids remains essentially unexplored. Inclusion bodies (IBs) are natural amyloids that occur as discrete protein nanoparticles in recombinant bacteria. These protein clusters have been recently explored as protein-based functional biomaterials with diverse biomedical applications, and adapted as nanopills to deliver recombinant protein drugs into mammalian cells. Interestingly, the slow protein release from IBs does not significantly affect the particulate organization and morphology of the material, suggesting the occurrence of a tight scaffold. Here, we have determined, by using a combined set of analytical approaches, a sponge-like supramolecular organization of IBs combining differently folded protein versions (amyloid and native-like), which supports both mechanical stability and sustained protein delivery. Apart from offering structural clues about how amyloid materials release their monomeric protein components, these findings open exciting possibilities for the tailored development of smart biofunctional materials, adapted to mimic the functions of amyloid-based secretory glands of higher organisms.",
keywords = "Biomaterial, Functional amyloid, Nanomedicine, Nanoparticles, Protein release",
author = "Olivia Cano-Garrido and Escarlata Rodr{\'i}guez-Carmona and C{\'e}sar D{\'i}ez-Gil and Esther V{\'a}zquez and Elisa Elizondo and Rafael Cubarsi and Joaquin Seras-Franzoso and Corchero, {Jos{\'e} Luis} and Ursula Rinas and Imma Ratera and Nora Ventosa and Jaume Veciana and Antonio Villaverde and Elena Garc{\'i}a-Fruit{\'o}s",
note = "Funding Information: The authors acknowledge the financial support from MICINN ( BFU2010-17450 and CTQ2010-19501 ), AGAUR ( 2009SGR-108 and 2009SGR00516 ) and CIBER en Bioingenier{\'i}a, Biomateriales y Nanomedicina, an initiative funded by the VI National R&D&i Plan 2008-2011, Iniciativa Ingenio 2010, Consolider Program, CIBER Actions and financed by the Instituto de Salud Carlos III with assistance from the European Regional Development Fund. We are also indebted to the Protein Production Platform (CIBER-BBN) for helpful technical assistance and for protein production and purification services ( http://www.bbn.ciber-bbn.es/programas/plataformas/equipamiento ). A.V. has been distinguished with an ICREA ACADEMIA award (from ICREA, Catalonia, Spain). O.C. was granted a beca lanzadera fellowship from CIBER-BBN and, at present, a FPU fellowship from MECD. E.G.F. is supported by the Programa Personal de T{\'e}cnico de Apoyo (Modalidad Infraestructuras cient{\'i}fico-tecnol{\'o}gicas, MICINN). J.S.F. is the recipient of a PIF doctoral fellowship from UAB. ",
year = "2013",
month = apr,
doi = "10.1016/j.actbio.2012.11.033",
language = "English",
volume = "9",
pages = "6134--6142",
journal = "Acta biomaterialia",
issn = "1742-7061",
publisher = "Elsevier BV",
number = "4",
}