Evidence map›Paper›PMID 35773549›Full record

ArticleMolecular diversity2023

Identification of potential matrix metalloproteinase-2 inhibitors from natural products through advanced machine learning-based cheminformatics approaches.

Ruoqi Yang, Guiping Zhao, Bin Cheng, Bin Yan

Abstract read
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In one paragraph

Article in Molecular diversity, 2023. 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
1.4field-weighted citation impact, top 17% 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

5 citing papers in PubMed, 9 citations in OpenAlex.

  1. Review
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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 at 2 institutions in 1 country.

Ruoqi YangShandong University of Traditional Chinese Medicine, Jinan, 250355, China. yangruoqia@163.com.
Guiping ZhaoShandong University of Traditional Chinese Medicine, Jinan, 250355, China.
Bin ChengAffiliated Hospital of Shandong University of Traditional Chinese Medicine, Jinan, 250355, China.
Bin YanShandong University of Traditional Chinese Medicine, Jinan, 250355, China. yanbinro2002@163.com.
Shandong University of Traditional Chinese Medicine · CNAffiliated Hospital of Shandong University of Traditional Chinese Medicine · CN

Funding

Sub-project of the National Ministry of Health Major New Drug Creation Science and Technology Major Project NO. 2014ZX09509001001
6 · The paper itself

Abstract

Matrix metalloproteinase-2 (MMP-2) is capable of degrading Collage TypeIV in the vascular basement membrane and extracellular matrix. Studies have shown that MMP-2 is tightly associated with the biological behavior of malignant tumors. Therefore, the identification of inhibitors targeting MMP-2 could be effective in treating the disease by maintaining extracellular matrix homeostasis. In the pharmaceutical and biomedical fields, many computational tools are widely used, which improve the efficiency of the whole process to some extent. Apart from the conventional cheminformatics approaches (e.g., pharmacophore model and molecular docking), virtual screening strategies based on machine learning also have promising applications. In this study, we collected 2871 compound activity data against MMP-2 from the ChEMBL database and divided the training and test sets in a 3:1 ratio. Four machine learning algorithms were then selected to construct the classification models, and the best-performing model, i.e., the stacking-based fusion model with the highest AUC value in both training and test datasets, was used for the virtual screening of ZINC database. Next, we screened 17 potential MMP-2 inhibitors from the results predicted by the machine learning model via ADME/T analysis. The interactions between these compounds and the target protein were explored through molecular docking calculations, and the results showed that ZINC712249, ZINC4270723, and ZINC15858504 had lower binding free energies than the co-crystal ligand. To further examine the binding stability of the complexes, we performed molecular dynamics simulations and finally identified these three hits as the most promising natural products for MMP-2 inhibitors.

Indexed as

Biological ProductsMatrix Metalloproteinase 2CheminformaticsMolecular Docking SimulationMolecular Dynamics SimulationQuantitative Structure-Activity RelationshipBiological ProductsMatrix Metalloproteinase 2CheminformaticsMachine learningMatrix metalloproteinase-2Natural productsVirtual screening

Identifiers

PMID35773549
OpenAlexW4283728533

What OpenQuestion holds

Textmetadata
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.