Structural and functional analysis of a homotrimeric collagen peptide.

OBJECTIVE

This study aimed to chemically synthesize a homotrimeric collagen peptide, evaluate its safety, and assess its effectiveness in promoting collagen synthesis.

METHODS

A homotrimeric collagen peptide was synthesized and structurally characterized using circular dichroism and infrared spectroscopy. Thermal stability was analyzed by TG-DSC, and molecular weight and amino acid composition were determined. cytotoxicity testing assessed safety, while UV-induced photoaging experiments evaluated its effects on collagen and elastin synthesis. studies in BALB/c mice examined its impact on collagen content, skin structure, and angiogenesis.

RESULTS

The synthesized collagen peptide exhibited high purity (99.1%) and an amino acid composition of glycine, proline, and hydroxyproline in a balanced ratio (15:17:13). Structural analysis confirmed a stable triple-helical conformation similar to type I collagen with excellent thermal stability (Tm = 326.15°C). Cytotoxicity testing showed no adverse effects on cell viability. , the peptide significantly enhanced collagen and elastin synthesis in fibroblasts. , intradermal and subcutaneous injection increased collagen content, improved skin structure, and enhanced microvessel density.

CONCLUSION

This study presents a chemically synthesized homotrimeric collagen peptide with superior purity, structural stability, and biological efficacy in promoting collagen synthesis. Compared to previous studies, this biomimetic material exhibits exceptional thermal stability (Tm = 326.15°C) and a well-balanced amino acid composition, enabling applications in cosmetics and medical devices requiring heat sterilization (e.g., autoclaving), as validated by our patented method (China Patent No. ZL202410309842.9).