ArticleApplied biochemistry and biotechnology2025
Characterization and Biological Performance of Anglerfish Collagen and Bovine Collagen.
Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
3 citing papers in PubMed.
- Collagen Scaffolds in Veterinary Medicine: Safety, Sustainability, and Clinical Accessibility of Mammalian- and Marine-Derived Sources-A Scoping Review.Animals : an open access journal from MDPI · 2026Review
- Collagen from Salted Jellyfish (Gels (Basel, Switzerland) · 2026Article
- Collagen from Bovine Omentum: Extraction and Characterization.Foods (Basel, Switzerland) · 2025Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
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.
Indexed as
Identifiers
41060586What Socratic holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.