Zhang Xinling, Li Kexin, Lu Nan, Takebayashi Takafumi, Zhou Boyu, Xie Hongbin, Li Yufan, Long Xingyun, Qin Xingjiong, Zhao Hongyi, Dong Jiying
Department of Plastic Surgery, Beijing Hospital, National Center of Gerontology, Beijing, China.
Institute of Geriatric Medicine, Chinese Academy of Medical Sciences, Beijing, China.
Front Bioeng Biotechnol. 2025 Apr 28;13:1575341. doi: 10.3389/fbioe.2025.1575341. eCollection 2025.
This study aimed to chemically synthesize a homotrimeric collagen peptide, evaluate its safety, and assess its effectiveness in promoting collagen synthesis.
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.
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.
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).
本研究旨在化学合成一种同三聚体胶原蛋白肽，评估其安全性，并评估其促进胶原蛋白合成的有效性。
合成一种同三聚体胶原蛋白肽，并使用圆二色光谱和红外光谱对其结构进行表征。通过热重-差示扫描量热法分析热稳定性，并测定分子量和氨基酸组成。细胞毒性测试评估安全性，而紫外线诱导的光老化实验评估其对胶原蛋白和弹性蛋白合成的影响。在BALB/c小鼠中进行的研究考察了其对胶原蛋白含量、皮肤结构和血管生成的影响。
合成的胶原蛋白肽纯度高（99.1%），甘氨酸、脯氨酸和羟脯氨酸的氨基酸组成比例平衡（15:17:13）。结构分析证实其具有与I型胶原蛋白相似的稳定三螺旋构象，热稳定性极佳（熔点=326.15°C）。细胞毒性测试表明对细胞活力无不良影响。此外，该肽显著增强了成纤维细胞中胶原蛋白和弹性蛋白的合成。此外，皮内和皮下注射增加了胶原蛋白含量，改善了皮肤结构，并提高了微血管密度。
本研究提出了一种化学合成的同三聚体胶原蛋白肽，其在促进胶原蛋白合成方面具有优异的纯度、结构稳定性和生物学功效。与先前的研究相比，这种仿生材料具有出色的热稳定性（熔点=326.15°C）和平衡的氨基酸组成，可应用于需要热灭菌（如高压灭菌）的化妆品和医疗器械中，这已通过我们的专利方法得到验证（中国专利号ZL202410309842.9）。
