Abstract
Elastin is an elastomeric, self‐assembling extracellular matrix protein with potential for use in biomaterials applications. Here, we compare the microstructural and tensile properties of the elastin‐based recombinant polypeptide (EP) EP20‐244 crosslinked with either genipin (GP) or pyrroloquinoline quinone (PQQ). Recombinant EP‐based sheets were produced via coacervation and subsequent crosslinking. The micron‐scale topography of the GP‐crosslinked sheets examined with atomic force microscopy revealed the presence of extensive mottling compared with that of the PQQ‐crosslinked sheets, which were comparatively smoother. Confocal microscopy showed that the subsurface porosity in the GP‐crosslinked sheets was much more open. GP‐crosslinked EP‐based sheets exhibited significantly greater tensile strength (P ≤ 0.05). Mechanistically, GP appears to yield a higher crosslink density than PQQ, likely due to its capacity to form short‐range and long‐range crosslinks. In conclusion, GP is able to strongly modulate the microstructural and mechanical properties of elastin‐based polypeptide biomaterials forming membranes with mechanical properties similar to native insoluble elastin. © 2006 Wiley Periodicals, Inc. Biopolymers 85: 199–206, 2007.
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