418
important asset of the intermediate fi lament model. In addition, the secondary
structure of intermediate fi lament proteins is dominated by an α-helical rod domain,
which very readily forms coiled coils with the proper polymerization partner.
The introspective nature of hydrogen bonding in α-helices makes these proteins less
likely to aggregate with other proteins than the far more gregarious spidroins, which
have a strong tendency to form β-sheets and β-sheet crystals. The spinning process
for artifi cial slime threads therefore only needs to align the α-helices and arrange the
proteins into a coherent fi bre. Once these conditions are met, subjecting the proteins
to modest stresses that exceed the yield stress (about 3 MPa) during draw processing
should open up the α-helices. This may allow for the formation of β-sheets among
adjacent proteins and the formation of a strong, tough protein fi bre,” (Fudge et al.
2010 ; see also Fudge et al. 2003 ).
Marine elastins are also discussed above. Although today fi sh elastins are
normally used as source for obtaining their hydrolysates for the cosmetic industry
(see for example Nishida et al. 2012 ), their biomimetic potential is absolutely
indisputable. Principles of marine elastin structural organization, and their physicchemical and material properties, determine current approaches where elastin-like
biocomposites are designed and used in tissue engineering (Wise et al. 2009 ;
Kothapalli and Ramamurthi 2009 ; Nivison-Smith et al. 2010 ; Girotti et al. 2011 ;
Prieto et al. 2011 ; Grover et al. 2012 ).
As discussed Waterhouse and co-workers ( 2011 ):
“In addition to its critical role in maintaining vessel integrity and elastic properties under pulsatile fl ow, elastin plays an important role in signalling and regulating
luminal endothelial and smooth muscle cells in the arterial wall. Despite its wellestablished signifi cance in the vasculature and its growing use as a biomaterial in
tissue engineering, the hemocompatibility of elastin is often overlooked. Past
studies pointing to the potential of arterial elastin and decellularized elastin as
nonthrombogenic materials have begun to be realized, with elastin scaffolds and
coatings displaying increased hemocompatibility.” (Waterhouse et al. 2011 ).
Recently, interesting results were reported by Shiratsuchi et al. ( 2010 ):
“it was showed that elastin peptides prepared from marine fi sh elastin inhibit collagen-induced platelet aggregation and stimulate migration and proliferation of human
skin fi broblasts. These results suggest that piscine elastin peptides can be applied as
useful biomaterials in which elasticity, antithrombotic property, and the enhancement
of cell migration and proliferation are required,” (Shiratsuchi et al. 2010 ).
13.1 Conclusion
In conclusion, I also take the liberty to concentrate your attention on polysaccharides
of marine vertebrate origin; by which I mean proteoglycans and glycosaminoglycans.
Proteoglycans (Tingbø et al. 2012 ) as well as glycosaminoglycans (GAGs) like
13 Marine Structural Proteins in Biomedicine and Tissue Engineering
important asset of the intermediate fi lament model. In addition, the secondary
structure of intermediate fi lament proteins is dominated by an α-helical rod domain,
which very readily forms coiled coils with the proper polymerization partner.
The introspective nature of hydrogen bonding in α-helices makes these proteins less
likely to aggregate with other proteins than the far more gregarious spidroins, which
have a strong tendency to form β-sheets and β-sheet crystals. The spinning process
for artifi cial slime threads therefore only needs to align the α-helices and arrange the
proteins into a coherent fi bre. Once these conditions are met, subjecting the proteins
to modest stresses that exceed the yield stress (about 3 MPa) during draw processing
should open up the α-helices. This may allow for the formation of β-sheets among
adjacent proteins and the formation of a strong, tough protein fi bre,” (Fudge et al.
2010 ; see also Fudge et al. 2003 ).
Marine elastins are also discussed above. Although today fi sh elastins are
normally used as source for obtaining their hydrolysates for the cosmetic industry
(see for example Nishida et al. 2012 ), their biomimetic potential is absolutely
indisputable. Principles of marine elastin structural organization, and their physicchemical and material properties, determine current approaches where elastin-like
biocomposites are designed and used in tissue engineering (Wise et al. 2009 ;
Kothapalli and Ramamurthi 2009 ; Nivison-Smith et al. 2010 ; Girotti et al. 2011 ;
Prieto et al. 2011 ; Grover et al. 2012 ).
As discussed Waterhouse and co-workers ( 2011 ):
“In addition to its critical role in maintaining vessel integrity and elastic properties under pulsatile fl ow, elastin plays an important role in signalling and regulating
luminal endothelial and smooth muscle cells in the arterial wall. Despite its wellestablished signifi cance in the vasculature and its growing use as a biomaterial in
tissue engineering, the hemocompatibility of elastin is often overlooked. Past
studies pointing to the potential of arterial elastin and decellularized elastin as
nonthrombogenic materials have begun to be realized, with elastin scaffolds and
coatings displaying increased hemocompatibility.” (Waterhouse et al. 2011 ).
Recently, interesting results were reported by Shiratsuchi et al. ( 2010 ):
“it was showed that elastin peptides prepared from marine fi sh elastin inhibit collagen-induced platelet aggregation and stimulate migration and proliferation of human
skin fi broblasts. These results suggest that piscine elastin peptides can be applied as
useful biomaterials in which elasticity, antithrombotic property, and the enhancement
of cell migration and proliferation are required,” (Shiratsuchi et al. 2010 ).
13.1 Conclusion
In conclusion, I also take the liberty to concentrate your attention on polysaccharides
of marine vertebrate origin; by which I mean proteoglycans and glycosaminoglycans.
Proteoglycans (Tingbø et al. 2012 ) as well as glycosaminoglycans (GAGs) like
13 Marine Structural Proteins in Biomedicine and Tissue Engineering