THESIS
2018
ix, 46, that is, xi, 46 pages : illustrations (chiefly color) ; 30 cm
Abstract
Mussel foot has been long studied for their adhesive properties in diverse conditions,
but it was until recently that these mussel foot proteins (Mfp) can be produced in the
recombinant form using bacterial expression systems. However, there are drawbacks
from using a bacterial system to express such proteins; some of which include:
insolubility, difficulty in purification, and the relatively large size of the full-length
protein. These difficulties can be avoided if only the functional portions of Mfp—the
minimized adhesive domains—can be utilized. However, the adhesive domains are short
in length, and they, when stand alone, may not be able to provide sufficient wet
adhesiveness as the full-length proteins do.
By inserting truncated adhesive domains derived from a mussel foot...[
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Mussel foot has been long studied for their adhesive properties in diverse conditions,
but it was until recently that these mussel foot proteins (Mfp) can be produced in the
recombinant form using bacterial expression systems. However, there are drawbacks
from using a bacterial system to express such proteins; some of which include:
insolubility, difficulty in purification, and the relatively large size of the full-length
protein. These difficulties can be avoided if only the functional portions of Mfp—the
minimized adhesive domains—can be utilized. However, the adhesive domains are short
in length, and they, when stand alone, may not be able to provide sufficient wet
adhesiveness as the full-length proteins do.
By inserting truncated adhesive domains derived from a mussel foot protein into the
amine and carboxyl termini and the middle of an elastin-like polypeptide, we created
TMfp: a recombinant protein that can form adhesive materials upon oxidation by
tyrosinase—an enzyme that post-translationally oxidizes tyrosine into the adhesive
moieties, DOPA. The resulting protein can not only serve as an adhesive interface but can
also form an entirely protein-based hydrogel.
The adhesive interface was shown to have adhesive properties to polymethyl
methacrylate (PMMA) and glass surfaces. Furthermore, the stiffness of TMfp
hydrogels can be modulated by using the coordination of DOPA-metal (e.g., Fe
3+ and
Ti
3+). The material was well suited for 3D cell culturing and exhibited excellent
cytocompatibility toward encapsulated human epithelial cells. This material has the
potential to be a biocompatible adhesive material for biomedical and research purposes.
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