Abstract：
:A recombinant silk-elastin-like protein copolymer SELP-47K containing tandemly repeated amino acid sequence blocks from silk, GAGAGS, and elastin, GVGVP, was fabricated into microdiameter fibers using a wet-spinning technique. Raman spectral analysis revealed the formation of antiparallel beta-sheet crystals of the silk-like blocks. Dry SELP-47K fibers display the dependence of mechanical properties such as Young's modulus on fiber diameter, suggesting more oriented and crystallized molecular chains in small-diameter fibers. Additionally, a brittle fracture mode was identified for dry fibers by SEM analysis of fracture surfaces. Hydration dramatically influenced the mechanical behavior of SELP-47K fibers. In contrast to the high tensile strength and limited strains to failure of dry fibers, fully hydrated SELP-47K fibers possessed strains to failure as high as 700%. Furthermore, upon chemical cross-linking, a tensile mechanical strength up to 20 MPa was achieved in hydrated fibers without compromising their high deformability. By combing the silk- and elastin-derived sequences into a single SELP-47K protein polymer, we demonstrated that protein fibers with high tensile strength and high deformability can be fabricated.
journal_name
Biomacromoleculesjournal_title
Biomacromoleculesauthors
Qiu W,Teng W,Cappello J,Wu Xdoi
10.1021/bm801296rsubject
Has Abstractpub_date
2009-03-09 00:00:00pages
602-8issue
3eissn
1525-7797issn
1526-4602pii
10.1021/bm801296rjournal_volume
10pub_type
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