Microstructural and tensile properties of elastin-based polypeptides crosslinked with genipin and pyrroloquinoline quinone.
Biopolymers
; 85(3): 199-206, 2007 Feb 15.
Article
in En
| MEDLINE
| ID: mdl-17066474
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 < or = 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.
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Database:
MEDLINE
Main subject:
Peptides
/
Elastin
/
Cross-Linking Reagents
/
Iridoids
/
PQQ Cofactor
Language:
En
Year:
2007
Type:
Article