Evidence map›Paper›PMID 40807236›Full record

ReviewMolecules (Basel, Switzerland)2025

Progress in Research on Animal Collagen Peptides: Preparation, Bioactivity, and Application.

Xuanxuan Ma, Po-Hsiang Chuang, Yu-Hui Tseng, Xiao Wang, Ziteng Ma, Haofei Chen, Wenye Zhai, Wenwen Yang, Zhaoqing Meng, Jing Xu

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. 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

10 authors.

Xuanxuan MaShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
Po-Hsiang ChuangCollege of Chemistry, Chemical Engineering and Environment, Minnan Normal University, Zhangzhou 363000, China.
Yu-Hui TsengCollege of Chemistry, Chemical Engineering and Environment, Minnan Normal University, Zhangzhou 363000, China.
Xiao WangShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.ORCID 0000-0003-4236-2483
Ziteng MaShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
Haofei ChenShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
Wenye ZhaiShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
Wenwen YangShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.
Zhaoqing MengShandong Hongjitang Pharmaceutical Group Co., Ltd., Jinan 250100, China.
Jing XuShandong Provincial Key Laboratory of Molecular Engineering, School of Chemistry and Chemical Engineering, Qilu University of Technology (Shandong Academy of Sciences), Jinan 250353, China.ORCID 0000-0003-0238-2025

Funding

National Natural Science Foundation of China No. 22178184Science, Education and Industry Integration Innovation Pilot Project from Qilu University of Technology (Shandong Academy of Sciences) 2024ZDZX12Shandong Provincial Natural Science Foundation, China ZR2021MB007, ZR2022MB099
6 · The paper itself

Abstract

Type I collagen is a major protein in animals, and its hydrolyzed products, collagen peptides, have wide-ranging applications. This article reviews collagen peptides' preparation methods, biological activities, and application progress in the fields of food, cosmetics, and medicine. By employing various extraction and hydrolysis methods, collagen peptides with different molecular weights can be obtained, and their biological activities are closely related to their molecular weight and amino acid sequence. Studies have revealed that collagen peptides possess a variety of biological activities, including antioxidant, hematopoietic promotion, osteogenic differentiation promotion, antihypertensive, and anti-diabetic effects. In the food industry, their antioxidant and hypoglycemic properties have opened new avenues for the development of healthy foods; in the cosmetics field, the moisturizing, anti-aging, and repair functions of collagen peptides are favored by consumers; in the medical field, collagen peptides are used in wound dressings, drug carriers, and tissue engineering scaffolds. Looking to the future, the development of green and efficient preparation technologies for collagen peptides and in-depth research into the relationship between their structure and function will be important research directions. The multifunctional properties of collagen peptides provide a broad prospect for their further application in the health industry.

Indexed as

CollagenPeptidesAnimalsAntioxidantsCosmeticsHumansTissue EngineeringAntioxidantsCollagenCosmeticsPeptidesbioactivitycollagen peptidespreparation

Identifiers

PMID40807236
PMCPMC12348636

What OpenQuestion holds

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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.