Evidence map›Paper›PMID 42507829›Full record

ArticleChemistry & biodiversity2026

Novel Triazole-Linked Xanthine-Steroid Hybrids: Molecular Docking and In Vitro Evaluation Against α-Glucosidase and MCF-7 Cells.

Diego Martinez, Guillermo E Negrón, Leydi Carrillo-Cocom, Alejandro Zepeda, Elsie Ramírez-Domínguez, Delfino Chamorro, Leticia Lomas, Rosa L Santillan, Susana Rincón, Alma Sánchez-Eleuterio

Abstract read
In one paragraph

Article in Chemistry & biodiversity, 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

10 authors.

Diego MartinezTecnológico Nacional de México, Unidad Mérida, Mérida, Yucatán, México.ORCID https://orcid.org/0009-0001-9694-078X
Guillermo E NegrónDepartamento de Ciencias Básicas, Universidad Autónoma Metropolitana Azcapotzalco, Ciudad de México, México.
Leydi Carrillo-CocomFacultad de Ingeniería Química, Universidad Autónoma de Yucatán, Merida, México.
Alejandro ZepedaFacultad de Ingeniería Química, Universidad Autónoma de Yucatán, Merida, México.
Elsie Ramírez-DomínguezDepartamento de Ciencias Básicas, Universidad Autónoma Metropolitana Azcapotzalco, Ciudad de México, México.
Delfino ChamorroDepartamento de Ciencias Básicas, Universidad Autónoma Metropolitana Azcapotzalco, Ciudad de México, México.
Leticia LomasDepartamento de Química, Universidad Autónoma Metropolitana Iztapalapa, Ciudad de México, México.
Rosa L SantillanDepartamento de Química, Avenida Instituto, Centro De Investigación y de Estudios Avanzados Del Instituto Politécnico Nacional, Ciudad de México, México.ORCID https://orcid.org/0000-0002-9279-7656
Susana RincónTecnológico Nacional de México, Unidad Mérida, Mérida, Yucatán, México.ORCID https://orcid.org/0000-0003-1485-5133
Alma Sánchez-EleuterioDepartamento de Ciencias Básicas, Universidad Autónoma Metropolitana Azcapotzalco, Ciudad de México, México.

Funding

Tecnologico Nacional de Mexico 24565.26-PUniversidad Autonoma Metropolitana CB012-19
6 · The paper itself

Abstract

Triazole hybrids have emerged as versatile scaffolds exhibiting diverse pharmacological profiles. In this study, four novel xanthine steroid hybrids linked via a 1,2,3-triazole moiety (4-7) were efficiently synthesized through copper(I)-catalyzed azide alkyne cycloaddition. Their bioactive potential was investigated using molecular docking and in vitro assays targeting both metabolic and apoptotic pathways. Docking simulations were performed against the anti-apoptotic protein BCL-2 (isoform 1), associated with human breast adenocarcinoma cells, and α-glucosidase, a key enzyme involved in carbohydrate hydrolysis. Among the series, compound 4 displayed the highest binding affinity toward α-glucosidase and significant affinity toward BCL-2. In vitro assays confirmed that compound 4 exhibited the most potent dual effect, demonstrating α-glucosidase inhibition with an IC

Indexed as

alpha-GlucosidasesAntineoplastic AgentsGlycoside Hydrolase InhibitorsMolecular Docking SimulationSteroidsTriazolesXanthineApoptosisCell ProliferationCell SurvivalDose-Response Relationship, DrugDrug Screening Assays, AntitumorHumansMCF-7 CellsMolecular StructureStructure-Activity Relationshipalpha-GlucosidasesAntineoplastic AgentsGlycoside Hydrolase InhibitorsSteroidsTriazolesXanthineanti‐cancer propertiescycloadditiondockingsteroid‐triazole‐xanthine based derivativesα‐glucosidase inhibitor

Identifiers

PMID42507829
PMCPMC13405439

What OpenQuestion holds

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Registered trials

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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.