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Vortex-induced injectable silk fibroin hydrogels.


ABSTRACT: A novel, to our knowledge, technique was developed to control the rate of beta-sheet formation and resulting hydrogelation kinetics of aqueous, native silk solutions. Circular dichroism spectroscopy indicated that vortexing aqueous solutions of silkworm silk lead to a transition from an overall protein structure that is initially rich in random coil to one that is rich in beta-sheet content. Dynamic oscillatory rheology experiments collected under the same assembly conditions as the circular dichroism experiments indicated that the increase in beta-sheet content due to intramolecular conformational changes and intermolecular self-assembly of the silk fibroin was directly correlated with the subsequent changes in viscoelastic properties due to hydrogelation. Vortexing low-viscosity silk solutions lead to orders-of-magnitude increase in the complex shear modulus, G*, and formation of rigid hydrogels (G* approximately 70 kPa for 5.2 wt % protein concentration). Vortex-induced, beta-sheet-rich silk hydrogels consisted of permanent, physical, intermolecular crosslinks. The hydrogelation kinetics could be controlled easily (from minutes to hours) by changing the vortex time, assembly temperature and/or protein concentration, providing a useful timeframe for cell encapsulation. The stiffness of preformed hydrogels recovered quickly, immediately after injection through a needle, enabling the potential use of these systems for injectable cell delivery scaffolds.

SUBMITTER: Yucel T 

PROVIDER: S-EPMC2756352 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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Vortex-induced injectable silk fibroin hydrogels.

Yucel Tuna T   Cebe Peggy P   Kaplan David L DL  

Biophysical journal 20091001 7


A novel, to our knowledge, technique was developed to control the rate of beta-sheet formation and resulting hydrogelation kinetics of aqueous, native silk solutions. Circular dichroism spectroscopy indicated that vortexing aqueous solutions of silkworm silk lead to a transition from an overall protein structure that is initially rich in random coil to one that is rich in beta-sheet content. Dynamic oscillatory rheology experiments collected under the same assembly conditions as the circular dic  ...[more]

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