THESIS
2017
x, 59 leaves : illustrations (some color) ; 30 cm
Abstract
Hydrogels have been serving as effective, multi-functional soft materials for
regenerative medicine for decades. Protein-based hydrogels enchanted with marvellous
tunability are now standing out as one of the most promising materials for biomedical
applications where stimuli responsiveness is critical. In this research, we explore the
feasibility of creating stimuli-responsive hydrogels by covalently assembling functional
protein molecules under mild conditions.
The central theme for modern molecular engineering is how to faithfully transfer the
function at the molecular level to the materials’ properties at the macroscopic level. To
achieve this, firstly, we developed a protein hydrogel comprising polymerized
calmodulins, a ubiquitously distributed protein family in biosphere...[
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Hydrogels have been serving as effective, multi-functional soft materials for
regenerative medicine for decades. Protein-based hydrogels enchanted with marvellous
tunability are now standing out as one of the most promising materials for biomedical
applications where stimuli responsiveness is critical. In this research, we explore the
feasibility of creating stimuli-responsive hydrogels by covalently assembling functional
protein molecules under mild conditions.
The central theme for modern molecular engineering is how to faithfully transfer the
function at the molecular level to the materials’ properties at the macroscopic level. To
achieve this, firstly, we developed a protein hydrogel comprising polymerized
calmodulins, a ubiquitously distributed protein family in biosphere that responds to
ambient Ca
2+ concentration accompanied with an induced conformational change and
substrate binding. The resulting materials possessed tuneable viscoelasticity varying
with the concentration of Ca
2+, indicating the alterations in macroscopic properties of
the materials were manoeuvred by Ca
2+ -triggered conformational change of
calmodulin. Further characterization has been accomplished and provided supportive
results on previous conclusion.
Adhesive materials of high biocompatibility and moisture resistance are of remarkable
demands in biomedical fields, especially for surgical applications. Inspired by the ultra-adhesive
byssal threads of marine mussels, two types of mussel foot proteins (MFPs)
were utilized to develop entirely protein-based hydrogels serving as bio-adhesives.
Recombinant bacterial tyrosinase from Streptomyces antibiotics were introduced for
the oxidization of tyrosine residues on MFPs to
L-3,4-dihydroxyphenylalanine (DOPA),
which can be further cross-linked with nucleophiles on the protein scaffolds. The
resulting materials show reliable adhesiveness as well as ideal mechanical properties
and biocompatibility, demonstrating the huge potential of MFP hydrogels as novel bio-adhesives
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