Evidence map›Paper›PMID 42715489›Full record

ArticleChemMedChem2026

Piano-Stool Ru (II) Complexes as Modulators of Human Prion Protein PrP

Rahul Chauhan, Himanshi Kumawat, Sakshi Saini, Abhishek Panwar, Prashant Kukreti, Nandita Medda, Partha Roy, Kaushik Ghosh

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Article in ChemMedChem, 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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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Rahul ChauhanDepartment of Chemistry, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.ORCID https://orcid.org/0009-0004-5438-3112
Himanshi KumawatDepartment of Chemistry, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.
Sakshi SainiDepartment of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.ORCID https://orcid.org/0009-0009-8376-1342
Abhishek PanwarDepartment of Chemistry, National Institute of Technology Manipur, Langol, Imphal, India.ORCID https://orcid.org/0009-0006-3351-0447
Prashant KukretiDepartment of Chemistry, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.ORCID https://orcid.org/0009-0005-3395-9482
Nandita MeddaDepartment of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.
Partha RoyDepartment of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.ORCID https://orcid.org/0000-0003-1943-3079
Kaushik GhoshDepartment of Chemistry, Indian Institute of Technology Roorkee, Roorkee, Uttarakhand, India.ORCID https://orcid.org/0000-0002-3792-2848

Funding

Anusandhan National Research Foundation
6 · The paper itself

Abstract

Prion diseases are neurodegenerative disorders caused by the accumulation of misfolded prion proteins, leading to neurotoxicity and neuronal death. Creutzfeldt-Jakob disease (CJD) in humans and Bovine spongiform encephalopathy (BSE) in animals are among the most prominent prion disorders. Therefore, the search for molecules that can serve as drugs for prion diseases has gained significant attention. In our study, we synthesised and characterised two piano-stool ruthenium complexes, RuBT and RuBI, based on benzazole-quinoline scaffolds. Molecular structures of RuBT and RuBI were determined by X-ray crystallography. The anti-aggregation effects of the complexes on PrP

Indexed as

Neuroprotective AgentsPeptide FragmentsPrion ProteinsPrionsRutheniumAnimalsCell SurvivalCrystallography, X-RayDose-Response Relationship, DrugHumansMiceMolecular Docking SimulationMolecular StructureProtein AggregatesStructure-Activity RelationshipNeuroprotective AgentsPeptide Fragmentsprion protein (106-126)Prion ProteinsPrionsProtein AggregatesRutheniumfibrillizationneurodegenerativeneuroprotectiveprion PrP106−126Ru(II) piano‐stool complexes

Identifiers

PMID42715489
PMCPMC13557631

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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.