Evidence map›Paper›PMID 39153161›Full record

ArticlePlant foods for human nutrition (Dordrecht, Netherlands)2024

Identification and Function Analysis of Novel Hypoglycemic and Antioxidant Peptides from Chickpea.

Pei Li, Guoping Chen, Rongyao Liang, Kaiwei Cai, Zihao Chen, Na Yang, Wenyi Huang, Zhiyong Xie, Yanlong Chen, Qiongfeng Liao

Abstract read
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In one paragraph

Article in Plant foods for human nutrition (Dordrecht, Netherlands), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Pro-Arg, The Potential Anti-Diabetes Peptide, Screened from Almond by In-Silico Analysis.Plant foods for human nutrition (Dordrecht, Netherlands) · 2025
    Article
  5. Review
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.

Pei Li *School of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Guoping Chen *School of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Rongyao Liang *School of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Kaiwei CaiSchool of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Zihao ChenSchool of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Na YangSchool of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Wenyi HuangSchool of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China.
Zhiyong XieSchool of Pharmaceutical Sciences (Shenzhen), Sun Yat-sen University, Shenzhen, 518106, Guangdong Province, China.
Yanlong ChenSchool of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China. chenyanlong@gzucm.edu.cn.
Qiongfeng LiaoSchool of Pharmaceutical Sciences, Guangzhou University of Chinese Medicine, Guangzhou, 510006, Guangdong Province, China. zyfxliao@gzucm.edu.cn.

Funding

the Guangdong Basic and Applied Basic Research Foundation No. 2024A1515011747the National Natural Science Foundation of China No. 22204029the National Natural Science Foundation of China No. 82074142the National Natural Science Foundation of China No. 82174104
6 · The paper itself

Abstract

Chickpea is rich in protein and has been demonstrated to possess hypoglycaemic effects. However, the specific bioactive ingredients and mechanisms underlying their hypoglycaemic effects remain unclear. In this study, enzymatic hydrolysis and gel permeation chromatography were used to extract chickpea bioactive peptide (CBP) from chickpea protein. One of the products, CBP-75-3, was found to inhibit α-glucosidase (GAA) activity and significantly increase the viability of insulin resistant (IR) cells. Moreover, CBP-75-3 significantly increased the rate of glucose consumption and glycogen synthesis in IR-HepG2 cells. Moreover, CBP-75-3 decreased the levels of malondialdehyde and increased the levels of superoxide dismutase, glutathione, and glutathione peroxidase. Subsequently, 29 novel bioactive peptides in CBP-75-3 were identified by LC‒MS/MS, and the potential hypoglycaemic targets of these novel bioactive peptides were investigated using molecular docking. Based on the results, the residues of the novel bioactive peptides interact with GAA through hydrogen bonding (especially LLR, FH, RQLPR, KGF and NFQ by binding to the substrate binding pocket or the active centre of GAA), thereby inhibiting GAA activity and laying a foundation for its hypoglycaemic activity. In short, the novel bioactive peptides isolated and identified from chickpea can effectively exert hypoglycaemic effects and increase the antioxidant capacity of IR-HepG2 cells. This study reveals that CBP-75-3, a natural hypoglycaemic ingredient, has potential for applications in functional foods and provides a theoretical basis for the development and application of CBP in the future.

Indexed as

AntioxidantsCicerHypoglycemic AgentsInsulin ResistanceMolecular Docking SimulationPeptidesalpha-GlucosidasesGlutathione PeroxidaseGlycoside Hydrolase InhibitorsHep G2 CellsHumansMalondialdehydePlant ProteinsSuperoxide DismutaseTandem Mass Spectrometryalpha-GlucosidasesAntioxidantsGlutathione PeroxidaseGlycoside Hydrolase InhibitorsHypoglycemic AgentsMalondialdehydePeptidesPlant ProteinsSuperoxide DismutaseAntioxidant capacityChickpeaHypoglycaemic peptidesInsulin resistanceMolecular docking

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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.