Typical structure, biocompatibility, and cell proliferation bioactivity of collagen from Tilapia and Pacific cod.

Aquatic collagens, as the alternative sources of mammalian collagen, have received increasing attention due to its low-cost, low-antigenicity, biocompatibility, and biodegradability. Pepsin-soluble collagens were extracted from the skins of Oreochromis mossambicus (Om-PSC) and Gadus macrocephalus (Gm-PSC), and their structural properties and bioactivities were probed to reveal their potential applications in biomedical material for tissue engineering. The results of Fourier transforms-infrared spectroscopy (FT-IR), circular dichroism (CD), X-ray diffraction (XRD), ultraviolet (UV) and sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) demonstrated that Om-PSC and Gm-PSC had similar and intact triple helical structures. The amino acid composition and peptide profiles revealed Om-PSC and Gm-PSC were identified as type I collagen with the typical repetitive sequence of (Gly-X-Y) n. However, the denaturation temperature (Td) was determined to be 29.7 ℃ of Om-PSC, much higher than that of Gm-PSC (17.3 ℃). Toxicological experiments demonstrated Om-PSC and Gm-PSC both had good biocompatibility and cytocompatibility, which met the requirements of medical materials. Fluorescence imaging and cell cycle distribution revealed Om-PSC and Gm-PSC could promote the proliferation of fibroblast and osteoblast cells. Therefore, Om-PSC and Gm-PSC showed the advantages in medical materials.