TY - JOUR

T1 - Supramolecular organization of protein-releasing functional amyloids solved in bacterial inclusion bodies

AU - Cano-Garrido, Olivia

AU - Rodríguez-Carmona, Escarlata

AU - Díez-Gil, César

AU - Vázquez, Esther

AU - Elizondo, Elisa

AU - Cubarsi, Rafael

AU - Seras-Franzoso, Joaquin

AU - Corchero, José Luis

AU - Rinas, Ursula

AU - Ratera, Imma

AU - Ventosa, Nora

AU - Veciana, Jaume

AU - Villaverde, Antonio

AU - García-Fruitós, Elena

N1 - Funding Information: The authors acknowledge the financial support from MICINN ( BFU2010-17450 and CTQ2010-19501 ), AGAUR ( 2009SGR-108 and 2009SGR00516 ) and CIBER en Bioingeniería, 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 Técnico de Apoyo (Modalidad Infraestructuras científico-tecnológicas, MICINN). J.S.F. is the recipient of a PIF doctoral fellowship from UAB.

PY - 2013/4

Y1 - 2013/4

N2 - 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.

AB - 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.

KW - Biomaterial

KW - Functional amyloid

KW - Nanomedicine

KW - Nanoparticles

KW - Protein release

UR - http://www.scopus.com/inward/record.url?scp=84875366908&partnerID=8YFLogxK

U2 - 10.1016/j.actbio.2012.11.033

DO - 10.1016/j.actbio.2012.11.033

M3 - Article

C2 - 23220450

AN - SCOPUS:84875366908

VL - 9

SP - 6134

EP - 6142

JO - Acta biomaterialia

JF - Acta biomaterialia

SN - 1742-7061

IS - 4

ER -