Biomedical Engineering Reference
In-Depth Information
14.6 CONCLUSION
11. Simnick AJ, Lim DW, Chow D, Chilkoti A. (2007) Bio-
medical and biotechnological applications of elastin-like
polypeptides. J. Macromol. Sci. C Poly. Rev. 47, 121-154.
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scopic study of the conformational transition of elastin-like
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14. Meyer DE, Chilkoti A. (2004) Quantification of the effects
of chain length and concentration on the thermal behavior
of elastin-like polypeptides. Biomacromolecules 5, 846-
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its gamma irradiation cross-linked matrix—summary of
generic biological
Recombinant protein expression is an important process but
cost-intensive process for the production of therapeutically
active biologics. ELPs derived from mammalian elastin are
extraordinarily biocompatible and they exhibit a thermally
responsive reversible soluble to insoluble phase transition.
These properties make ELPs attractive for drug delivery, as
materials for tissue repair or engineering, or to facilitate the
purification of recombinant ELP-fusion proteins by a pro-
cess termed inverse phase transition. Recently, plant-based
expression systems have been evaluated for the production
of ELP-fusion proteins. The simplified purification and the
great potential of transgenic plants as bioreactors open new
possibilities for the large-scale production of recombinant
proteins such as biopharmaceuticals and industrial enzymes.
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