Structural effects of crosslinking a biopolymer hydrogel derived from marine mussel adhesive protein
Weisser, J. T.
Wilker, J. J.
Google Scholar check
MetadataShow full item record
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. © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.
Showing items related by title, author, creator and subject.
Antoniades, Ioanna; Stylianou, Panayiota; Christodoulou, Neophytos; Skourides, Paris A. (2017)We previously identified focal adhesion kinase (FAK) as an important regulator of ciliogenesis in multiciliated cells. FAK and other focal adhesion (FA) proteins associate with the basal bodies and their striated rootlets ...
Split-Inteins for Simultaneous, site-specific conjugation of Quantum Dots to multiple protein targets In vivo Charalambous, Anna; Antoniades, Ioanna; Christodoulou, Neophytos; Skourides, Paris A. (2011)Background: Proteins labelled with Quantum Dots (QDs) can be imaged over long periods of time with ultrahigh spatial and temporal resolution, yielding important information on the spatiotemporal dynamics of proteins within ...
Kypri, Elena; Christodoulou, A.; Maimaris, G.; Lethan, M.; Markaki, M.; Lysandrou, C.; Lederer, C. W.; Tavernarakis, N.; Geimer, S.; Pedersen, L. B.; Santama, Niovi (2014)Nucleotide-binding proteins Nubp1 and Nubp2 are MRP/MinD-type P-loop NTPases with sequence similarity to bacterial division site-determining proteins and are conserved, essential proteins throughout the Eukaryotes. They ...