Abstract
Recombinant elastin-based proteins (ELPs) are used in applications that include therapeutics, drug delivery, and tissue engineering due to their biocompatibility and unique ability to undergo simple coacervation. Here, we describe a cost-effective method to purify ELPs utilizing salt precipitation and their reversible phase transition property when heated above their lower critical solution temperature (LCST). Furthermore, we describe the post-translational modification of converting tyrosine residues to L-3,4-dihydroxyphenylalanine (DOPA) for adhesive applications.
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