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Cooperative behavior of a sacrificial bond network and elastic framework in providing self-healing capacity in mussel byssal threads.
Reinecke, Antje; Bertinetti, Luca; Fratzl, Peter; Harrington, Matthew J.
Afiliación
  • Reinecke A; Dept. of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.
  • Bertinetti L; Dept. of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.
  • Fratzl P; Dept. of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany.
  • Harrington MJ; Dept. of Biomaterials, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany. Electronic address: matt.harrington@mpikg.mpg.de.
J Struct Biol ; 196(3): 329-339, 2016 12.
Article en En | MEDLINE | ID: mdl-27477391
The dissipative and self-healing properties of mussel byssal threads are critical for their function as anchoring fibers in wave-battered habitats and central to their emergence as an exciting model system for bio-inspired polymers. Much is now understood about the structure-function relationships defining this remarkable proteinaceous bio-fiber; however, the molecular mechanisms underlying the distinctive tough, viscoelastic and self-healing behavior are still unclear. Here, we investigate elastic and dissipative contributions from the primary load-bearing proteins in the distal region of byssal threads (the preCols) using X-ray diffraction (XRD) combined with in situ tensile testing. Specifically, we identified cross ß-sheet structure in the preCol flanking domains that functions as an elastic framework, providing hidden length. Dissipative behavior was associated with a strain-rate dependent phase transition of a sacrificial network stabilized by strong, reversible cross-links. Based on these findings, we posit a new model for byssal thread deformation and self-healing.
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Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Relación Estructura-Actividad / Biopolímeros / Proteínas / Conformación Proteica en Lámina beta Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Alemania

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Relación Estructura-Actividad / Biopolímeros / Proteínas / Conformación Proteica en Lámina beta Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 2016 Tipo del documento: Article País de afiliación: Alemania