Correlation between Mechanical Properties of Three Freshwater Fish Skin Collagen Films and the Primary Structure of the α1Chain in Collagen
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Abstract:
The study aimed to investigate the correlation between mechanical properties of three freshwater fish skin collagen films and the primary structure of the collagen α1 chain (COL1A1). The results showed that the tensile strength of tilapia skin collagen films reached up to 51.24 MPa, which was higher than those of the silver carp and grass carp skin films. Moreover, the color values of tilapia skin collagen films were closer to those of a white standard plate. Significant differences were observed in the ratios of positive to negative peak (RPN) calculated from the circular dichroism (CD) spectra of the three types of fish collagen solutions, while similar RPN values were observed in the resulting collagen films. Furthermore, the silver carp COL1A1 gene sequence was cloned using reverse transcription-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE). The 4923-bp full-length cDNA of silver carp COL1A1 (GenBank No. KJ848743) was obtained, which encoded 1448 amino acids. The constructed phylogenetic tree showed that the COL1A1 sequences of silver carp and grass carp clustered together, but were distant from that of tilapia. The analysis of the primary structure of COL1A1 indicated that there were more proline residues in the C-peptide and G-X-Y sequences of the triple-helical domain of tilapia COL1A1; therefore, strong collagen films could be formed using tilapia skins.
