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    Por favor, use este identificador para citar o enlazar este ítem:http://uvadoc.uva.es/handle/10324/24448

    Título
    Intrafibrillar Mineralization of Self-Assembled Elastin-Like Recombinamer Fibrils
    Autor
    Li, Yuping
    Rodríguez Cabello, José CarlosAutoridad UVA Orcid
    Aparicio, Conrado
    Año del Documento
    2017
    Editorial
    American Chemical Society
    Descripción
    Producción Científica
    Documento Fuente
    ACS Applied Materials & Interfaces, 2017, 9 (7), pp 5838–5846
    Résumé
    Biomineralization of bone, a controlled process where hydroxyapatite nanocrystals preferentially deposit in collagen fibrils, is achieved by the interplay of the collagen matrix and noncollagenous proteins. Mimicking intrafibrillar mineralization in synthetic systems is highly attractive for the development of advanced hybrid materials with elaborated morphologies and outstanding mechanical properties, as well as understanding the mechanisms of biomineralization. Inspired by nature, intrafibrillar mineralization of collagen fibrils has been successfully replicated in vitro via biomimetic systems, where acidic polymeric additives are used as analogue of noncollagenous proteins in mediating mineralization. The development of synthetic templates that mimic the structure and functions of collagenous matrix in mineralization has yet to be explored. In this study, we demonstrated that self-assembled fibrils of elastin-like recombinamers (ELRs) can induce intrafibrillar mineralization. The ELRs displayed a disordered structure at low temperature but self-assembled into nanofibrils above its inverse transition temperature. In the presence of the self-assembled ELR fibrils, polyaspartate-stabilized amorphous calcium phosphates preferentially infiltrated into the fibrils and then crystallized into hydroxyapatite nanocrystals with their [001] axes aligned parallel to the long axis of the ELR fibril. As the recombinant technology enables designing and producing well-defined ELRs, their molecular and structural properties can be fine-tuned. By examining the ultrastructure of the self-assembled ELRs fibrils as well as their mineralization, we concluded that the spatial confinement formed by a continuum β-spiral structure in an unperturbed fibrillar structure rather than electrostatic interactions or bioactive sequences in the recombinamer composition played the crucial role in inducing intrafibrillar mineralization.
    Palabras Clave
    Calcificación
    Mineralización
    Revisión por pares
    SI
    DOI
    10.1021/acsami.6b15285
    Patrocinador
    Ministerio de Economía, Industria y Competitividad (Project MAT2013-42473-R and MAT2015-68901R)
    Junta de Castilla y León (programa de apoyo a proyectos de investigación – Ref. VA244U13, VA313U14 and VA015U16)
    Patrocinador
    info:eu-repo/grantAgreement/EC/H2020/646075
    info:eu-repo/grantAgreement/EC/H2020/642687
    info:eu-repo/grantAgreement/EC/FP7/278557
    info:eu-repo/grantAgreement/EC/FP7/317306
    Version del Editor
    http://pubs.acs.org/doi/abs/10.1021/acsami.6b15285
    Idioma
    eng
    URI
    http://uvadoc.uva.es/handle/10324/24448
    Derechos
    openAccess
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    • BIOFORGE - Artículos de revista [89]
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    Attribution-NonCommercial-NoDerivatives 4.0 InternationalExcepté là où spécifié autrement, la license de ce document est décrite en tant que Attribution-NonCommercial-NoDerivatives 4.0 International

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