Level D· Scientific groundwork from lab and animal studiesAnimal StudyEurope PMCOpen access

Valorization of <i>Channa striatus</i> waste skin for developing marine collagen peptide based hydrogels for potential wound dressings

Tarannum T., Islam F., Shariar KK., Islam N.

Animal Study on Chronic Wound, Burns, Chronic Inflammation, published in RSC Adv (2025) — summary generated from the PubMed abstract.

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Level D· Scientific groundwork from lab and animal studiesEvidence level of this study

Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.

  • Level A · Stronger Clinical Evidence
  • Level B · Emerging clinical evidence with positive signals
  • Level C · Early human research exploring benefits
  • Level D · Scientific groundwork from lab and animal studies
  • Emerging · Emerging topic under active research
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This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.

Study type
Animal Study
Journal
RSC Adv (2025)
Reported sample size
—
Source database
Europe PMC
PMID
41122407
PMCID
PMC12536424
DOI
10.1039/d5ra05717e

Abstract (original English)

This study focuses on the extraction and characterization of a bioactive collagen peptide from waste skin of a local species of fish, the Channa striatus /snakehead/'shol' fish. The extracted peptides were characterized and optimized for the formulation of chitosan/PVA/collagen peptide (CP) hydrogel which has not been done previously. The facile extraction process involved using alkali, butanol, and protease for non-collagenous protein and fat removal, and enzymatic hydrolysis respectively. Hydrogels were formulated using a non-toxic freeze-thaw technique with multiple combinations of chitosan, PVA, and collagen peptide and characterized with SEM, FTIR, swelling ratio, gel content, porosity, evaporation rate, and antibacterial and anti-inflammatory activity. The FTIR fingerprint of the collagen peptide confirmed the presence of characteristic amide bonds. The SEM image of the collagen peptide reveals an open morphological structure suggesting that enzymatic hydrolysis could produce lower molecular weight collagen peptide. The collagen peptide retained 53.31% total protein in which essential amino acids - 27.3% glycine, 8.74% arginine, and 14.11% proline - were present. Antioxidant properties - DPPH, hydroxide, and superoxide radical scavenging activity - demonstrated a linear correlation with collagen peptide concentration. The swelling ratio, a crucial structural property for

What this study does not prove

  • • This study does not prove SVF is an approved treatment or a replacement for standard care.
  • • This is preclinical work; animal or laboratory results cannot be applied to humans.

Evidence level

Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.

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