Mechanistic Insights into Pancreatic Lipase Inhibition by Pea-Derived Peptides: Integrating Process Optimization, Activity Assays, Docking, and Molecular Dynamics.

Yi Zhao, Jinhong Wang, Xiang Li, Guizhao Liang

Abstract read

In one paragraph

Article in Foods (Basel, Switzerland), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Yi ZhaoKey Laboratory of Biorheological Science and Technology, Ministry of Education, Bioengineering College, Chongqing University, Chongqing 400044, China.

Jinhong WangKey Laboratory of Biorheological Science and Technology, Ministry of Education, Bioengineering College, Chongqing University, Chongqing 400044, China.

Xiang LiKey Laboratory of Biorheological Science and Technology, Ministry of Education, Bioengineering College, Chongqing University, Chongqing 400044, China.

Guizhao LiangKey Laboratory of Biorheological Science and Technology, Ministry of Education, Bioengineering College, Chongqing University, Chongqing 400044, China.

Funding

Chongqing Talent Program Project cstc2024ycjh-bgzxm0113National Natural Science Foundation of China 32172196Technology Innovation and Application Development Key Project of Chongqing CSTB2024TIAD-KPX0014

6 · The paper itself

Abstract

Pancreatic lipase (PL) plays a central role in dietary lipid digestion and is a promising target for food-derived inhibitors. In this study, pea protein hydrolysates (PPHs) with PL inhibitory activity were prepared by enzymatic hydrolysis and characterized for their functional and peptidomic properties. Compared with pea protein isolate, PPH showed lower surface hydrophobicity, and moderate antioxidant activity. Peptidomic analysis identified 1740 peptides in the active hydrolysate. Combined in silico screening and in vitro validation further identified three peptides, GFSL, WFE, and FGF, as effective PL inhibitors, with IC

Indexed as

inhibitory peptidesMM/PBSAmolecular dynamics simulationspancreatic lipasestructure–activity relationship

Identifiers

PMID42121466

DOI10.3390/foods15091523

PMCPMC13163611

What OpenQuestion holds

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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.