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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Bioinspired self-assembly of tyrosinase-modified silicatein and fluorescent core-shell silica spheres
T A Elkhooly1, W E G Müller, X Wang
1Institute of Physiological Chemistry, Duesbergweg 6, University Medical Center, Johannes Gutenberg-University, Mainz, Germany. Biomaterials Department, National Research Centre, Dokki, Cairo, Egypt.
Abstract:
Inspired by the intermolecular cross-linking of mussel foot proteins and their adhesive properties, tyrosinase has been used to modify recombinant silicatein. DOPA/DOPAquinone-mediated cross-linking and interfacial interactions enhanced both self-assembly of silicatein building blocks and templating of core-shell silica spheres, resulting in fluorescent biomimetic silicatein-silica hybrid mesofibers.

