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Article

Easily accessible polycyclic amines that inhibit the wild-type and amantadine-resistant mutants of the M2 channel of influenza A virus.

Journal of medicinal chemistry - 10 Jul 2014

Rey-Carrizo Matias, Barniol-Xicota Marta, Ma Chunlong, Frigolé-Vivas Marta, Torres Eva, Naesens Lieve, Llabrés Salomé, Juárez-Jiménez Jordi, Luque Francisco J, DeGrado William F, Lamb Robert A, Pinto Lawrence H, Vázquez Santiago

Abstract excerpt

Amantadine inhibits the M2 proton channel of influenza A virus, yet most of the currently circulating strains of the virus carry mutations in the M2 protein that render the virus amantadine-resistant. While most of the research on novel amantadine analogues has revolved around the synthesis of novel adamantane derivatives, we have recently found that other polycyclic scaffolds effectively block the M2 proton...

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Identifiers

PMID: 24941437
DOI: 10.1021/jm5005804
PMCID: PMC4096222

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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