Evidence map›Paper›PMID 40357327›Full record

ArticleFrontiers in bioengineering and biotechnology2025

Structural and functional analysis of a homotrimeric collagen peptide.

Xinling Zhang, Kexin Li, Nan Lu, Takafumi Takebayashi, Boyu Zhou, Hongbin Xie, Yufan Li, Xingyun Long, Xingjiong Qin, Hongyi Zhao and 1 more

Abstract read
In one paragraph

Article in Frontiers in bioengineering and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Preparation and Characterization of Eel (Foods (Basel, Switzerland) · 2025
    Article
  4. Antibiotics (Basel, Switzerland) · 2025
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors.

Xinling Zhang *Department of Plastic Surgery, Beijing Hospital, National Center of Gerontology, Beijing, China.
Kexin Li *LivingPhoenix Regenerative Technologies Development (Chengdu) Co., Ltd., Chengdu, China.
Nan LuSkinVision Lab, Shanghai Institute of Plastic Surgery and Aesthetic Medicine Industrial Innovation, Shanghai, China.
Takafumi TakebayashiLivingPhoenix Regenerative Technologies Development (Chengdu) Co., Ltd., Chengdu, China.
Boyu ZhouLivingPhoenix Regenerative Technologies Development (Chengdu) Co., Ltd., Chengdu, China.
Hongbin XieDepartment of Plastic Surgery, Peking University Third Hospital, Beijing, China.
Yufan LiLivingPhoenix Regenerative Technologies Development (Chengdu) Co., Ltd., Chengdu, China.
Xingyun LongSichuan Academy of Social Sciences, Sichuan, China.
Xingjiong QinLivingPhoenix Regenerative Technologies Development (Chengdu) Co., Ltd., Chengdu, China.
Hongyi ZhaoDepartment of Plastic Surgery, Beijing Hospital, National Center of Gerontology, Beijing, China.
Jiying DongDepartment of Plastic and Reconstructive Surgery, Shanghai Ninth People's Hospital, Shanghai Jiaotong University of Medicine, Shanghai, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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. 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. 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).

Indexed as

collagen peptidesheat stabilityhomotrimersafetysynthesis

Identifiers

PMID40357327
PMCPMC12066645

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.