Evidence map›Paper›PMID 38601950›Full record

ArticleFood chemistry: X2024

Identification and characterization of a calcium-binding peptide from salmon bone for the targeted inhibition of α-amylase in digestion.

Zhe Xu, Shiying Han, Na Cui, Hanxiong Liu, Xu Yan, Hongrui Chen, Jianping Wu, Zhijian Tan, Ming Du, Tingting Li

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Food chemistry: X, 2024. 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
0.9field-weighted citation impact, top 27% of its field
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, 4 citations in OpenAlex.

  1. Review
  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 at 6 institutions in 2 countries.

Zhe XuCollege of Life Sciences, Key Laboratory of Biotechnology and Bioresources Utilization, Dalian Minzu University, Ministry of Education, Dalian 116600, China.
Shiying HanCollege of Life Sciences, Key Laboratory of Biotechnology and Bioresources Utilization, Dalian Minzu University, Ministry of Education, Dalian 116600, China.
Na CuiDepartment of Food and Chemical Engineering, Liuzhou Institute of Technology, Liuzhou, Guangxi 545616, China.
Hanxiong LiuSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, China.
Xu YanCollege of Life Sciences, Key Laboratory of Biotechnology and Bioresources Utilization, Dalian Minzu University, Ministry of Education, Dalian 116600, China.
Hongrui ChenSchool of Food and Bioengineering, Food Microbiology Key Laboratory of Sichuan Province, Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, Xihua University, Chengdu, Sichuan 611130, China.
Jianping WuDepartment of Agricultural, Food and Nutritional Science, University of Alberta, Edmonton, Alberta T6G2P5, Canada.
Zhijian TanInstitute of Bast Fiber Crops & Center of Southern Economic Crops, Chinese Academy of Agricultural Sciences, Changsha 410205, China.
Ming DuSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, China.
Tingting LiCollege of Life Sciences, Key Laboratory of Biotechnology and Bioresources Utilization, Dalian Minzu University, Ministry of Education, Dalian 116600, China.
Dalian Minzu University · CNDalian Polytechnic University · CNUniversity of Alberta · CAInstitute of Bast Fiber Crops · CNMinzu University of China · CNXihua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Amylase, essential for carbohydrate digestion, relies on calcium (Ca) for its structural integrity and enzymatic activity. This study explored the inhibitory effect of salmon bone peptides on α-amylase activity through their interaction with the enzyme's Ca-binding sites. Among the various salmon bone hydrolysates, salmon bone trypsin hydrolysate (SBTH) exhibited the highest α-amylase inhibition. The peptide IEELEEELEAER (PIE), with a sequence of Ile-Glu-Glu-Leu-Glu-Glu-Glu-Glu-Leu-Glu-Ala-Glu-Arg from SBTH, was found to specifically target the Ca-binding sites in α-amylase, interacting with key residues such as Asp206, Trp203, His201, etc. Additionally, cellular experiments using 3 T3-L1 preadipocytes indicated PIE's capability to suppress adipocyte differentiation, and decreases in intracellular triglycerides, total cholesterol, and lipid accumulation. In vivo studies also showed a significant reduction in weight gain in the group treated with PIE(6.61%)compared with the control group (33.65%). These findings suggest PIE is an effective α-amylase inhibitor, showing promise for obesity treatment.

Indexed as

Calcium-bindingPeptideSalmon boneTargeted inhibitionα-amylase

Identifiers

PMID38601950
PMCPMC11004067
OpenAlexW4393857696

What Socratic holds

Textmetadata
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 Socratic graph.