Meier, C and Welland, ME (2011) Wet-spinning of amyloid protein nanofibers into multifunctional high-performance biofibers. Biomacromolecules, 12. pp. 3453-3459.Full text not available from this repository.
Amyloid nanofibers derived from hen egg white lysozyme were processed into macroscopic fibers in a wet-spinning process based on interfacial polyion complexation using a polyanionic polysaccharide as cross-linker. As a result of their amyloid nanostructure, the hierarchically self-assembled protein fibers have a stiffness of up to 14 GPa and a tensile strength of up to 326 MPa. Fine-tuning of the polyelectrolytic interactions via pH allows to trigger the release of small molecules, as demonstrated with riboflavin-5'-phophate. The amyloid fibrils, highly oriented within the gellan gum matrix, were mineralized with calcium phosphate, mimicking the fibrolamellar structure of bone. The formed mineral crystals are highly oriented along the nanofibers, thus resulting in a 9-fold increase in fiber stiffness.
|Uncontrolled Keywords:||Amyloidogenic Proteins Animals Biocompatible Materials Calcium Phosphates Chickens Cross-Linking Reagents Flavin Mononucleotide Hydrogen-Ion Concentration Microscopy, Electron, Scanning Muramidase Nanofibers Polymers Polysaccharides, Bacterial Surface Properties Tensile Strength Tissue Engineering|
|Divisions:||Div B > Solid State Electronics and Nanoscale Science|
|Depositing User:||Cron Job|
|Date Deposited:||18 May 2016 17:47|
|Last Modified:||25 May 2016 23:45|