Abstract
ABSTRACTWe describe the biosynthesis and characterization of protein materials comprised of two distinct self-assembling domains (SADs): elastin (E) found in tissue for its elastic properties and cartilage oligomeric matrix protein coiled-coil (COMPcc, C) predominantly locatedin joint and in bones. Based on earlier studies on protein block polymers comprised these two SADs, orientation and number of blocks play a crucial role in the overall stimuli-responsive supramolecular assembly behavior. Here we fabricate a range of EnC and CEn block polymers in which the E domain is systematically truncated to explore the effects of the E domain on the overall physicochemical behavior.
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