Comprehensive assessment of Nile tilapia skin collagen sponges as hemostatic dressings.

Nile tilapia skin collagen sponge was fabricated by lyophilization and cross-linked with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide in the presence of N-hydroxysuccinimide (EDC/NHS). The physicochemical properties were examined. The EDC/NHS cross-linked collagen sponge presented an enhanced water absorption capacity. In addition, biocompatibility and hemostatic efficiency were evaluated by acute systemic toxicity assay, dermal irritation test, intradermal reaction test, sensitization test, cytotoxicity, blood clotting assay in vitro, and liver and femoral artery hemorrhage models in vivo. Results showed that the produced collagen sponges before and after EDC/NHS cross-linking had excellent biocompatibility. Furthermore, EDC/NHS cross-linking promoted fibroblast cells viability and proliferation reflected by the MTT reduction assay. Meanwhile, EDC/NHS cross-linked collagen sponge exhibited the best blood clotting ability and hemostatic efficiency in rat femoral artery hemorrhage model in comparison with non-crosslinked and commercial collagen sponges. Our results demonstrated that the fabricated collagen sponges could be used as perfect hemostatic dressings.

In vitro assessment of the multifunctional bioactive potential of Alaska pollock skin collagen following simulated gastrointestinal digestion.

BACKGROUND: Dietary mineral deficiency, hypertension and diabetes have become serious human health problems. Dietary approaches are increasingly being investigated to address these issues. Identification of food-derived biological peptides has become an important approach to control such diseases. Peptides generated from aquatic byproducts have been shown to possess biological activities. RESULTS: Significantly higher copper-chelating activity was observed on simulated hydrolysis of intact collagen. The collagen hydrolysate generated in the gastric stage exhibited moderate angiotensin-converting enzyme (ACE)-inhibitory activity with an IC50 value of 2.92 ± 0.22 mg mL(-1), which significantly decreased to 0.49 ± 0.02 mg mL(-1) after intestinal digestion. The dipeptidyl peptidase (DPP) IV-inhibitory potency of the collagen hydrolysate generated directly following simulated gastrointestinal digestion (SGID) (IC50 2.59 ± 0.04 mg mL(-1)) was significantly lower than that of the collagen tryptic hydrolysate (CTH) (IC50 1.53 ± 0.01 mg mL(-1)). The antioxidant activities of collagen and CTH using the ferric-reducing antioxidant power (FRAP) assay were 0.87 ± 0.10 and 1.27 ± 0.03 µmol Trolox equivalent (TE) g(-1) respectively after SGID. CONCLUSION: This study identifies collagen as a good and inexpensive substrate for the generation of biologically active peptides with potential applications as functional ingredients in the management of chronic illness and mineral deficiency problems.