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.
authors.affiliation: Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, Bellaterra, 08193 Barcelona, Spain.
authors.forename: Olivia
authors.initials: O
authors.lastname: Cano-Garrido
authors.forename: Escarlata
authors.initials: E
authors.lastname: Rodríguez-Carmona
authors.forename: César
authors.initials: C
authors.lastname: Díez-Gil
authors.forename: Esther
authors.initials: E
authors.lastname: Vázquez
authors.forename: Elisa
authors.initials: E
authors.lastname: Elizondo
authors.forename: Rafael
authors.initials: R
authors.lastname: Cubarsi
authors.forename: Joaquin
authors.initials: J
authors.lastname: Seras-Franzoso
authors.forename: José Luis
authors.initials: JL
authors.lastname: Corchero
authors.forename: Ursula
authors.initials: U
authors.lastname: Rinas
authors.forename: Imma
authors.initials: I
authors.lastname: Ratera
authors.forename: Nora
authors.initials: N
authors.lastname: Ventosa
authors.forename: Jaume
authors.initials: J
authors.lastname: Veciana
authors.forename: Antonio
authors.initials: A
authors.lastname: Villaverde
authors.forename: Elena
authors.initials: E
authors.lastname: García-Fruitós
mesh_terms: D058227:Amyloidogenic Proteins / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000648:ultrastructure; D004926:Escherichia coli / Q000737:chemistry* / Q000648:ultrastructure; D002479:Inclusion Bodies / Q000737:chemistry* / Q000648:ultrastructure; D046911:Macromolecular Substances / Q000737:chemistry; D008422:Materials Testing; D008968:Molecular Conformation; D010316:Particle Size; D013499:Surface Properties
chemical_list: D058227:Amyloidogenic Proteins; D001426:Bacterial Proteins; D046911:Macromolecular Substances