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<p>Collagen plays a crucial role in maintaining the structural stability and functional integrity of vertebrates. The currently extracted animal-derived collagens include those from mammalian and marine sources. In this study, a comparative analysis was conducted to examine the differences between marine-derived (anglerfish) and mammalian-derived collagen (bovine). Both types of collagen can form a porous fibrous network through&#xa0;in vitro self-assembly. Further analysis using UV–vis, FT-IR, CD and SDS-PAGE confirmed that both collagens were typical Type I collagen, maintaining an intact triple-helix structure. DSC and TGA results showed that the thermal denaturation temperature of anglerfish collagen was markedly lower than that of bovine collagen. Both types of collagen are hydrophilic materials. Amino acid composition analysis demonstrated significant differences in proline and serine content. Type I collagenase degrades anglerfish collagen faster than bovine collagen. Both collagen variants enhanced cellular growth without inducing hemolysis, exhibiting outstanding biocompatibility. In conclusion, marine-derived collagen demonstrates high structural and functional similarity to mammalian collagen. The degradation and biocompatibility of collagen make it promising for hemostasis, wound dressings, and drug delivery. These results provide a scientific foundation for the efficient utilization and sustainable development of marine collagen resources.</p> Graphical Abstract <p></p>

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Characterization and Biological Performance of Anglerfish Collagen and Bovine Collagen

  • 期刊论文

  • 发表日期：

    2025年10月8日

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  • Hanxiao Song,
  • Baoheng Yin,
  • Bing Jiang,
  • Lian Mi,
  • Chang Cui,
  • Wen Su,
  • Na Bai

摘要

Collagen plays a crucial role in maintaining the structural stability and functional integrity of vertebrates. The currently extracted animal-derived collagens include those from mammalian and marine sources. In this study, a comparative analysis was conducted to examine the differences between marine-derived (anglerfish) and mammalian-derived collagen (bovine). Both types of collagen can form a porous fibrous network through in vitro self-assembly. Further analysis using UV–vis, FT-IR, CD and SDS-PAGE confirmed that both collagens were typical Type I collagen, maintaining an intact triple-helix structure. DSC and TGA results showed that the thermal denaturation temperature of anglerfish collagen was markedly lower than that of bovine collagen. Both types of collagen are hydrophilic materials. Amino acid composition analysis demonstrated significant differences in proline and serine content. Type I collagenase degrades anglerfish collagen faster than bovine collagen. Both collagen variants enhanced cellular growth without inducing hemolysis, exhibiting outstanding biocompatibility. In conclusion, marine-derived collagen demonstrates high structural and functional similarity to mammalian collagen. The degradation and biocompatibility of collagen make it promising for hemostasis, wound dressings, and drug delivery. These results provide a scientific foundation for the efficient utilization and sustainable development of marine collagen resources.

Graphical Abstract