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Structural Effects of Crosslinking a Biopolymer Hydrogel Derived from Marine Mussel Adhesive Protein
Author(s) -
Loizou Elena,
Weisser Jaime T.,
Dundigalla Avinash,
Porcar Lionel,
Schmidt Gudrun,
Wilker Jonathan J.
Publication year - 2006
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200600097
Subject(s) - biopolymer , self healing hydrogels , small angle x ray scattering , nanometre , micrometer , viscoelasticity , chemical engineering , materials science , adhesive , rheology , neutron scattering , scattering , nanotechnology , chemistry , polymer chemistry , composite material , polymer , physics , layer (electronics) , optics , engineering
Summary: In an effort to explore new biocompatible substrates for biomedical technologies, we present a structural study on a crosslinked gelatinous protein extracted from marine mussels. Prior studies have shown the importance of iron in protein crosslinking and mussel adhesive formation. Here, the structure and properties of an extracted material were examined both before and after crosslinking with iron. The structures of these protein hydrogels were studied by SEM, SANS, and SAXS. Viscoelasticity was tested by rheological means. The starting gel was found to have a heterogeneous porous structure on a micrometer scale and, surprisingly, a regular structure on the micron to nanometer scale. However disorder, or “no periodic structure”, was deduced from scattering on nanometer length scales at very high q . Crosslinking with iron condensed the structure on a micrometer level. On nanometer length scales at high q , small angle neutron scattering showed no significant differences between the samples, possibly due to strong heterogeneity. X‐ray scattering also confirmed the absence of any defined periodic structure. Partial crosslinking transformed the viscoelastic starting gel into one with more rigid and elastic properties.Environmental scanning electron micrographs of the protein gel after crosslinking with iron.