Literature DB >> 26511069

Rational approach to an antiprion compound with a multiple mechanism of action.

Maria Laura Bolognesi1, Salvatore Bongarzone2, Suzana Aulic3, Hoang Ngoc Ai Tran4, Federica Prati1, Paolo Carloni5, Giuseppe Legname3.   

Abstract

BACKGROUND: The main pathogenic event of prion disorders has been identified in the deposition of the disease-associated prion protein (PrP(Sc)), which is accompanied by metal dyshomeostasis.
RESULTS: The multitarget-directed ligand 1, designed by combining a heteroaromatic prion recognition motif to an 8-hydroxyquinoline metal chelator, has been developed as a potential antiprion disease-modifying agent. Importantly, 1 was found to effectively clear PrP(Sc) from scrapie-infected cells, and, at the same time, inhibit metal-induced prion aggregation and reactive oxygen species generation. 1 was also characterized in terms of pharmacokinetic properties in a preliminary in vitro investigation.
CONCLUSION: Compound 1 has emerged as a suitable lead candidate against prion diseases and as a good starting point for a further optimization process.

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Year:  2015        PMID: 26511069     DOI: 10.4155/fmc.15.79

Source DB:  PubMed          Journal:  Future Med Chem        ISSN: 1756-8919            Impact factor:   3.808


  2 in total

1.  A Promising Antiprion Trimethoxychalcone Binds to the Globular Domain of the Cellular Prion Protein and Changes Its Cellular Location.

Authors:  N C Ferreira; L M Ascari; A G Hughson; G R Cavalheiro; C F Góes; P N Fernandes; J R Hollister; R A da Conceição; D S Silva; A M T Souza; M L C Barbosa; F A Lara; R A P Martins; B Caughey; Y Cordeiro
Journal:  Antimicrob Agents Chemother       Date:  2018-01-25       Impact factor: 5.191

Review 2.  Therapeutic strategies for identifying small molecules against prion diseases.

Authors:  Elisa Uliassi; Lea Nikolic; Maria Laura Bolognesi; Giuseppe Legname
Journal:  Cell Tissue Res       Date:  2022-01-06       Impact factor: 5.249

  2 in total

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