Reversible hydrogels from self-assembling genetically engineered protein block copolymers.
A series of triblock protein copolymers composed of a central water-soluble polyelectrolyte segment flanked by two coiled-coil domains was synthesized by genetic engineering methods. The copolymers self-assembled into reversible hydrogels in response to changes in temperature, pH, and the presence or absence of denaturating agent (guanidine hydrochloride, GdnHCl). Hydrogel formation was concentration-dependent, and the concentration needed for hydrogel formation correlated with the oligomerization state of the coiled-coil domains in the protein copolymers. The morphology of the hydrogels, as determined by scanning electron microscopy (SEM), indicated the presence of porous interconnected networks. The thermal stabilities and self-assembling properties of the protein copolymers were successfully controlled by manipulating the amino acid sequences of the coiled-coil domains. The stimuli responsiveness and reversibility of the hydrogel self-assembly suggest that these protein copolymers may have potential in biomedical applications.
Xu
Chunyu
C
Department of Pharmaceutics and Pharmaceutical Chemistry and of Bioengineering, University of Utah, Salt Lake City, Utah 84112, USA.
Breedveld
Victor
V
Kopecek
Jindrich
J
D000595:Amino Acid Sequence / Q000235:genetics; D020100:Hydrogels / Q000138:chemical synthesis*; D008969:Molecular Sequence Data; D011108:Polymers / Q000138:chemical synthesis*; D015202:Protein Engineering / Q000379:methods*; D011506:Proteins / Q000138:chemical synthesis* / Q000235:genetics*
D020100:Hydrogels; D011108:Polymers; D011506:Proteins