321
© Springer Science+Business Media Dordrecht 2015
H. Ehrlich, Biological Materials of Marine Origin, Biologically- Inspired Systems 4,
DOI 10.1007/978-94-007-5730-1_8
Chapter 8
Marine Collagens
Abstract There are three main categories of marine collagens: collagens of
invertebrate origin (sponges, jellyfi sh, molluscs), fi sh collagens, and marine mammal collagens. Marine fi sh collagens isolated from skin, meat, scales, fi ns and waste
materials are of particular interest from an industrial point of view. Different types
of fi sh collagen-based biomaterials (gels, scaffolds, sponges, fi lms, membranes,
composites) and their biomedical application are discussed in this chapter.
Collagens are structural proteins, defi nitively, of fundamental evolutionary
signifi cance in both marine invertebrates and in vertebrate taxa. All of them possess
a characteristic structural element in the form of rod-like triple-helical segment,
however differ otherwise in their size, and functional roles. “As a family of proteins
with unique structural features, marine invertebrate collagens have been a focus of
structure–function correlation studies; as well as studies interrelating successive
levels of structural organization, from the amino acid sequence to the anatomically
defi ned fi bril,” (Ehrlich 2010 ). Numerous review papers (e.g., Gross et al. 1956 ;
Engel 1997 ; Garrone 1999 ; Exposito et al. 2002 ) and books (e.g., Garrone 1978 ;
Bairati and Garrone 1985 ; Ehrlich 2010 ) are dedicated entirely to collagens of
marine invertebrates like sponges, corals, worms, molluscs, echinoderms, and crustaceans. Using a gentle, alkali-based slow-etching method we have recently isolated
fi brillar collagens from Hyalonema sieboldi and Monorhaphis chuni glass sponges.
The isolated organic fraction is revealed to be dominated by a hydroxylated fi brillar
collagen that contains an unusual [Gly-3Hyp-4Hyp] motif (Ehrlich et al. 2010 ).
Hydroxylated collagen appears to form the basis for the specifi c optical and extraordinary mechanical properties of hexactinellid specular structures.
The self-assembly properties of collagen and its templating activity for silicifi cation processes are useful for inspiring current ideas about the development of hierarchical silica-based architectures. Macroscopic bundles of silica nanostructures result
from the kinetic cross-coupling of two molecular processes: a dynamic supramolecular self-assembly, and a stabilizing silica mineralization. The feedback interactions
between template growth and inorganic deposition are driven non-enzymatically by
means of hydrogen bonding. We speculate that the hydroxylated glass sponge collagen may change the nature of silica in aqueous solution by converting the distribution
of oligomers to an arrangement favourable for the mineralization. We suggest that
© Springer Science+Business Media Dordrecht 2015
H. Ehrlich, Biological Materials of Marine Origin, Biologically- Inspired Systems 4,
DOI 10.1007/978-94-007-5730-1_8
Chapter 8
Marine Collagens
Abstract There are three main categories of marine collagens: collagens of
invertebrate origin (sponges, jellyfi sh, molluscs), fi sh collagens, and marine mammal collagens. Marine fi sh collagens isolated from skin, meat, scales, fi ns and waste
materials are of particular interest from an industrial point of view. Different types
of fi sh collagen-based biomaterials (gels, scaffolds, sponges, fi lms, membranes,
composites) and their biomedical application are discussed in this chapter.
Collagens are structural proteins, defi nitively, of fundamental evolutionary
signifi cance in both marine invertebrates and in vertebrate taxa. All of them possess
a characteristic structural element in the form of rod-like triple-helical segment,
however differ otherwise in their size, and functional roles. “As a family of proteins
with unique structural features, marine invertebrate collagens have been a focus of
structure–function correlation studies; as well as studies interrelating successive
levels of structural organization, from the amino acid sequence to the anatomically
defi ned fi bril,” (Ehrlich 2010 ). Numerous review papers (e.g., Gross et al. 1956 ;
Engel 1997 ; Garrone 1999 ; Exposito et al. 2002 ) and books (e.g., Garrone 1978 ;
Bairati and Garrone 1985 ; Ehrlich 2010 ) are dedicated entirely to collagens of
marine invertebrates like sponges, corals, worms, molluscs, echinoderms, and crustaceans. Using a gentle, alkali-based slow-etching method we have recently isolated
fi brillar collagens from Hyalonema sieboldi and Monorhaphis chuni glass sponges.
The isolated organic fraction is revealed to be dominated by a hydroxylated fi brillar
collagen that contains an unusual [Gly-3Hyp-4Hyp] motif (Ehrlich et al. 2010 ).
Hydroxylated collagen appears to form the basis for the specifi c optical and extraordinary mechanical properties of hexactinellid specular structures.
The self-assembly properties of collagen and its templating activity for silicifi cation processes are useful for inspiring current ideas about the development of hierarchical silica-based architectures. Macroscopic bundles of silica nanostructures result
from the kinetic cross-coupling of two molecular processes: a dynamic supramolecular self-assembly, and a stabilizing silica mineralization. The feedback interactions
between template growth and inorganic deposition are driven non-enzymatically by
means of hydrogen bonding. We speculate that the hydroxylated glass sponge collagen may change the nature of silica in aqueous solution by converting the distribution
of oligomers to an arrangement favourable for the mineralization. We suggest that