Structural aspects of fish skin collagen which forms ordered arrays via liquid crystalline states.
The ability of acid-soluble type I collagen extracts from Soleidae flat fish to form ordered arrays in condensed phases has been compared with data for calf skin collagen. Liquid crystalline assemblies in vitro are optimized by preliminary treatment of the molecular population with ultrasounds. This treatment requires the stability of the fish collagen triple helicity to be controlled by X-ray diffraction and differential scanning calorimetry and the effect of sonication to be evaluated by viscosity measurements and gel electrophoresis. The collagen solution in concentrations of at least 40 mg ml(-1) showed in polarized light microscopy birefringent patterns typical of precholesteric phases indicating long-range order within the fluid collagen phase. Ultrastructural data, obtained after stabilization of the liquid crystalline collagen into a gelated matrix, showed that neutralized acid-soluble fish collagen forms cross-striated fibrils, typical of type I collagen, following sine wave-like undulations in precholesteric domains. These ordered geometries, approximating in vivo situations, give interesting mechanical properties to the material.
Giraud-Guille
M M
MM
Observatoire Océanologique, Histo-Cytophysique EPHE, Université P. et M. Curie and CNRS-UMR 7628, France. mmgg@arago.obs-banyuls.fr
Besseau
L
L
Chopin
C
C
Durand
P
P
Herbage
D
D
D000818:Animals; D002152:Calorimetry, Differential Scanning; D002417:Cattle; D003094:Collagen / Q000737:chemistry* / Q000648:ultrastructure; D003460:Crystallization; D005399:Fishes; D008854:Microscopy, Electron; D011487:Protein Conformation; D012867:Skin / Q000737:chemistry* / Q000648:ultrastructure; D014961:X-Ray Diffraction
D003094:Collagen