Dependence of Self-Assembled Peptide Hydrogel Network Structure on Local Fibril Nanostructure
Citations Over TimeTop 12% of 2009 papers
Abstract
Physically cross-linked, fibrillar hydrogel networks are formed by the self-assembly of β-hairpin peptide molecules with varying degrees of strand asymmetry. The peptide registry in the self-assembled state can be used as a design element to generate fibrils with twisting, nontwisting, or laminated morphology. The mass density of the networks varies significantly, and can be directly related to the local fibrillar morphology as evidenced by small angle neutron scattering (SANS) and in situ substantiation using cryogenic transmission electron microscopy (cryo-TEM) under identical concentrations and conditions. Similarly, the density of the network is dependent on changes in the peptide concentration. Bulk rheological properties of the hydrogels can be correlated to the fibrillar nanostructure, with the stiffer, laminated fibrils forming networks with a higher G' as compared to the flexible, singular fibrillar networks.
Related Papers
- → Small-angle neutron scattering on polymer gels: phase behavior, inhomogeneities and deformation mechanisms(2010)224 cited
- → A More Informative Approach for Characterization of Polymer Monolithic Phases: Small Angle Neutron Scattering/Ultrasmall Angle Neutron Scattering(2011)14 cited
- → Fractal aggregation in silica sols in basic tetraethoxysilane/ethanol/water solutions by small-angle neutron scattering(2020)6 cited
- → Introduction to Small-angle X-ray and Neutron Scattering(2000)3 cited
- → Fundamental theory in small-angle scattering: X-ray and neutron(2023)