Studies on the mechanism of collagen fibril assembly in fish scales

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Using MS analysis, scale SLRPs, which were possible regulators of 3-dimensinal architecture of teleost fish collagen, were identified. After the cDNA cloning of SLRPs, localization of their mRNAs were clarified. We also revealed a negative correlation between collagen denaturation temperature (DT) and contents of α3-subunit, as well as positive correlation between DT and hydroxylation ratio of proline residues in the collagen. Thus, these two factors seem to be the major regulators of DT of fish collagen. Artificial fibrillogenesis of collagen under magnetic field enabled a synthesis of a material having relatively aligned collagen fibrils, whose viscoelasticity and tensile strength were highest under 4 T and 12 T, respectively. High-density meso-porous new material was also synthesized using fish collagen.