Study On The Correlation Between Mechanical Properties And ¦¡1 Chain Primary Structure Of Three Freshwater Fish Skin Collagen Membranes
Keywords
Freshwater Fish Collagen Films Mechanical Properties Circular Dichroism Spectra Cloning Triple-Helical Domain Freshwater Fish Collagen Films Mechanical Properties Circular Dichroism Spectra Cloning Triple-Helical Domain
Abstract
This article explores the correlation between the mechanical properties of three freshwater fish skin collagen films and the primary structure of collagen ¦Á1 chains. The results showed that the tensile strength of the protein film prepared using tilapia skin collagen can reach 51.24 MPa, which is higher than that of protein films prepared from silver carp and grass carp skin collagen, and the color is closer to white. There are obvious differences in the absolute values (RPN values) of the positive and negative absorption peak intensity ratios in the circular dichroism spectra (CD spectra) of the three types of fish skin collagen solutions, but the RPN values in the CD spectra of the collagen films are relatively close. On the other hand, the silver carp collagen ¦Á1 chain (COL1A1) gene was cloned using RT-PCR and RACE methods, and the full length of COL1A1 cDNA was obtained, 4923 bp (NCBI sequence number: KJ848743), encoding 1448 amino acids; phylogenetic tree analysis results showed that The COL1A1 sequences of silver carp and grass carp belong to the same branch and are genetically distant from tilapia. According to the analysis results of the primary structure of the ¦Á1 chain of three collagens, it was found that the C-propeptide and the GXY sequence in the triple helical domain of the tilapia collagen ¦Á1 chain contain more Pro, so the tilapia skin collagen can form a high-strength protein membrane. The study aimed to investigate the correlation between mechanical properties of three freshwater fish skin collagen films and the primary structure of the collagen ¦Á1 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 GXY sequences of the triple-helical domain of tilapia COL1A1; therefore, strong collagen films could be formed using tilapia skins.
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Original research was done by Tang Lanlan
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