Evidence map›Paper›PMID 41165462›Full record

ArticleChemistry & biodiversity2026

Novel Yunaconitine Derivatives as Protein Tyrosine Phosphatase 1B Inhibitors and Radical Scavenger: Design, Synthesis, in Vitro Cellular Evaluation, and Molecular Docking Study.

Enxiao Wang, Lin Xing, Lulu Li, Meidi Deng, Yuxin Ding, Chaoyan Zhang, Wenhui Wu, Ruilong Sheng, Long Huang, Yong Shen and 1 more

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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.

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2 · The registry

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4 · The record

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5 · Who and what money

Authors and funding

11 authors.

Enxiao WangCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Lin XingCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Lulu LiCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Meidi DengCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Yuxin DingCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Chaoyan ZhangCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Wenhui WuCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.
Ruilong ShengCQM - Centro de Química da Madeira, Universidade Da Madeira, Campus da Penteada, Funchal, Portugal.
Long HuangZhejiang Cicheng Pharmaceutical Co., Ltd., Hangzhou, China.
Yong ShenDepartment, Institution, Address College of Agriculture and Biotechnology, Yunnan Agricultural University, Kunming, P. R. China.
Ruihua GuoCollege of Food Science and Technology, Shanghai Ocean University, Shanghai, China.ORCID https://orcid.org/0000-0001-8414-886X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Diabetes and oxidative stress are serious threats to human health and well-being. Protein tyrosine phosphatase 1B (PTP1B) and oxidative stress are important targets for managing diabetes. In this work, a series of new Yunaconitine derivatives (1-25) were synthesized and characterized; their inhibitory activity on PTP1B was first evaluated. Among them, derivatives 2 and 25 showed remarkable bioactivities with half-maximal inhibitory concentration values of 7.724 and 8.981 µM, respectively. Furthermore, derivatives 2 and 25 were evaluated for their free radical scavenging activity in vitro. Notably, derivative 25 exhibited significant free radical scavenging: 50% effective concentration = 58.76 µM. In addition, molecular docking analysis indicated that derivative 25 has a binding affinity for PTP1B and nicotinamide adenine dinucleotide phosphate-oxidase, with a binding energy of -5.03 and -2.66 kcal/mol, respectively. These results suggested that derivative 25 possesses great potential as a dual-target (PTP1B Inhibitor and radical scavenger) drug candidate for the treatment of diabetes.

Indexed as

AconitineDrug DesignEnzyme InhibitorsFree Radical ScavengersMolecular Docking SimulationProtein Tyrosine Phosphatase, Non-Receptor Type 1Dose-Response Relationship, DrugHumansMolecular StructureStructure-Activity RelationshipAconitineEnzyme InhibitorsFree Radical ScavengersProtein Tyrosine Phosphatase, Non-Receptor Type 1PTPN1 protein, humanDPPH free radical scavenging activitydual‐target inhibitormolecular dockingPTP1B inhibitorYunaconitine derivatives

Identifiers

PMID41165462
PMCPMC13420634

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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.