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ORIGINAL RESEARCH article
Front. Bioeng. Biotechnol.
Sec. Biomaterials
Volume 13 - 2025 | doi: 10.3389/fbioe.2025.1575341
Structural and Functional Analysis of a Homotrimeric Collagen Peptide
Provisionally accepted
Xinling Zhang1Kexin Li2Nan Lu3Takafumi Takebayashi2Boyu Zhou2Hongbin Xie4Yufan Li2Xingyun Long5Xingjiong Qin2Hongyi Zhao1*
Jiying Dong6*- 1Beijing Hospital, National Center of Gerontology, Beijing, China
- 2LivingPhoenix Regenerative Technologies Development (Chengdu) Co., Ltd., Chengdu, China
- 3Shanghai Institute of Plastic Surgery & Aesthetic Medicine Industrial Innovation, Shanghai, China
- 4Peking University Third Hospital, Haidian, Beijing Municipality, China
- 5Sichuan Academy of Social Sciences, Chengdu, Sichuan Province, China
- 6Shanghai Ninth People’s Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, China
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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. In vitro cytotoxicity testing assessed safety, while UV-induced photoaging experiments evaluated its effects on collagen and elastin synthesis. In vivo 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. In vitro, the peptide significantly enhanced collagen and elastin synthesis in fibroblasts. In vivo, 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).
Keywords: Collagen peptides, homotrimer, Synthesis, Heat stability, Safety
Received: 12 Feb 2025; Accepted: 11 Apr 2025.
Copyright: © 2025 Zhang, Li, Lu, Takebayashi, Zhou, Xie, Li, Long, Qin, Zhao and Dong. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence:
Hongyi Zhao, Beijing Hospital, National Center of Gerontology, Beijing, China
Jiying Dong, Shanghai Ninth People’s Hospital, Shanghai Jiaotong University School of Medicine, Shanghai, China
Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.