Evidence map›Paper›PMID 37836621›Full record

ArticleMolecules (Basel, Switzerland)2023

Theoretical Studies for the Discovery of Potential Sucrase-Isomaltase Inhibitors from Maize Silk Phytochemicals: An Approach to Treatment of Type 2 Diabetes.

Linda-Lucila Landeros-Martínez, Mara Ibeth Campos-Almazán, Nora-Aydeé Sánchez-Bojorge, Raul Flores, Juan Pedro Palomares-Báez, Luz María Rodríguez-Valdez

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 6 citations in OpenAlex.

  1. Trial
  2. Article
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  4. 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

6 authors at 1 institution in 1 country.

Linda-Lucila Landeros-MartínezFacultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Chihuahua 31125, Mexico.
Mara Ibeth Campos-AlmazánFacultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Chihuahua 31125, Mexico.ORCID 0000-0003-0654-3199
Nora-Aydeé Sánchez-BojorgeFacultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Chihuahua 31125, Mexico.
Raul FloresFacultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Chihuahua 31125, Mexico.ORCID 0000-0003-3845-1555
Juan Pedro Palomares-BáezFacultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Chihuahua 31125, Mexico.
Luz María Rodríguez-ValdezFacultad de Ciencias Químicas, Universidad Autónoma de Chihuahua, Chihuahua 31125, Mexico.ORCID 0000-0002-4954-2631
Autonomous University of Chihuahua · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A theoretical analysis of the potential inhibition of human sucrase-isomaltase (SI) by flavonoids was carried out with the aim of identifying potential candidates for an alternative treatment of type 2 diabetes. Two compounds from maize silks, maysin and luteolin, were selected to be studied with the structure-based density functional theory (DFT), molecular docking (MDock), and molecular dynamics (MD) approaches. The docking score and MD simulations suggested that the compounds maysin and luteolin presented higher binding affinities in N-terminal sucrase-isomaltase (NtSI) than in C-terminal sucrase-isomaltase (CtSI). The reactivity parameters, such as chemical hardness (η) and chemical potential (µ), of the ligands, as well as of the active site amino acids of the NtSI, were calculated by the meta-GGA M06 functional in combination with the 6-31G(d) basis set. The lower value of chemical hardness calculated for the maysin molecule indicated that this might interact more easily with the active site of NtSI, in comparison with the values of the acarbose and luteolin structures. Additionally, a possible oxidative process was proposed through the quantum chemical calculations of the electronic charge transfer values (∆N) between the active site amino acids of the NtSI and the ligands. In addition, maysin displayed a higher ability to generate more oxidative damage in the NtSI active site. Our results suggest that maysin and luteolin can be used to develop novel α-glucosidase inhibitors via NtSI inhibition.

Indexed as

Diabetes Mellitus, Type 2Amino AcidsHumansLuteolinMolecular Docking SimulationOligo-1,6-GlucosidasePhytochemicalsSucraseZea maysAmino AcidsLuteolinOligo-1,6-GlucosidasePhytochemicalsSucraseacarboseluteolinmaysinmolecular dockingmolecular dynamicsquantum chemicalsucrose-isomaltase

Identifiers

PMID37836621
PMCPMC10574772
OpenAlexW4386996955

What Socratic 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 Socratic graph.