Synthesis and preclinical evaluation of [

EAI045 EGFR Epidermal growth factor receptor TKI Tyrosine kinase inhibitor

Journal

EJNMMI research
ISSN: 2191-219X
Titre abrégé: EJNMMI Res
Pays: Germany
ID NLM: 101560946

Informations de publication

Date de publication:
16 Feb 2024
Historique:
received: 08 08 2023
accepted: 02 02 2024
medline: 16 2 2024
pubmed: 16 2 2024
entrez: 16 2 2024
Statut: epublish

Résumé

Mutations in the epidermal growth factor receptor (EGFR) kinase domain are common in non-small cell lung cancer. Conventional tyrosine kinase inhibitors target the mutation site in the ATP binding pocket, thereby inhibiting the receptor's function. However, subsequent treatment resistance mutations in the ATP binding site are common. The EGFR allosteric inhibitor, EAI045, is proposed to have an alternative mechanism of action, disrupting receptor signaling independent of the ATP-binding site. The antibody cetuximab is hypothesized to increase the number of accessible allosteric pockets for EAI045, thus increasing the potency of the inhibitor. This work aimed to gain further knowledge on pharmacokinetics, the EGFR mutation-targeting potential, and the influence of cetuximab on the uptake by radiolabeling EAI045 with carbon-11 and tritium. 2-(5-fluoro-2-hydroxyphenyl)-2-((2-iodobenzyl)amino)-N-(thiazol-2-yl)acetamide and 2-(5-fluoro-2-hydroxyphenyl)-N-(5-iodothiazol-2-yl)-2-(1-oxoisoindolin-2-yl)acetamide were synthesized as precursors for the carbon-11 and tritium labeling of EAI045, respectively. [ EAI045 was successfully labeled with tritium and carbon-11, and the in vivo results indicated [

Sections du résumé

BACKGROUND BACKGROUND
Mutations in the epidermal growth factor receptor (EGFR) kinase domain are common in non-small cell lung cancer. Conventional tyrosine kinase inhibitors target the mutation site in the ATP binding pocket, thereby inhibiting the receptor's function. However, subsequent treatment resistance mutations in the ATP binding site are common. The EGFR allosteric inhibitor, EAI045, is proposed to have an alternative mechanism of action, disrupting receptor signaling independent of the ATP-binding site. The antibody cetuximab is hypothesized to increase the number of accessible allosteric pockets for EAI045, thus increasing the potency of the inhibitor. This work aimed to gain further knowledge on pharmacokinetics, the EGFR mutation-targeting potential, and the influence of cetuximab on the uptake by radiolabeling EAI045 with carbon-11 and tritium.
RESULTS RESULTS
2-(5-fluoro-2-hydroxyphenyl)-2-((2-iodobenzyl)amino)-N-(thiazol-2-yl)acetamide and 2-(5-fluoro-2-hydroxyphenyl)-N-(5-iodothiazol-2-yl)-2-(1-oxoisoindolin-2-yl)acetamide were synthesized as precursors for the carbon-11 and tritium labeling of EAI045, respectively. [
CONCLUSIONS CONCLUSIONS
EAI045 was successfully labeled with tritium and carbon-11, and the in vivo results indicated [

Identifiants

pubmed: 38363422
doi: 10.1186/s13550-024-01078-6
pii: 10.1186/s13550-024-01078-6
doi:

Types de publication

Journal Article

Langues

eng

Pagination

19

Subventions

Organisme : H2020 Marie Skłodowska-Curie Actions
ID : 675417

Informations de copyright

© 2024. The Author(s).

Références

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Auteurs

Antonia A Högnäsbacka (AA)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands. a.hognasbacka@amsterdamumc.nl.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands. a.hognasbacka@amsterdamumc.nl.

Alex J Poot (AJ)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Christophe Plisson (C)

Invicro LLC, London, W12 0NN, UK.

Jonas Bergare (J)

Early Chemical Development, Pharmaceutical Sciences, R&D AstraZeneca, Gothenburg, Sweden.

David R Bonsall (DR)

Invicro LLC, London, W12 0NN, UK.

Stuart P McCluskey (SP)

Invicro LLC, London, W12 0NN, UK.

Lisa A Wells (LA)

Invicro LLC, London, W12 0NN, UK.

Esther Kooijman (E)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Robert C Schuit (RC)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Mariska Verlaan (M)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Wissam Beaino (W)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Guus A M S van Dongen (GAMS)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Danielle J Vugts (DJ)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Charles S Elmore (CS)

Early Chemical Development, Pharmaceutical Sciences, R&D AstraZeneca, Gothenburg, Sweden.

Jan Passchier (J)

Invicro LLC, London, W12 0NN, UK.

Albert D Windhorst (AD)

Department Radiology and Nuclear Medicine, Vrije Universiteit Amsterdam, Amsterdam UMC, De Boelelaan 1117, 1081HV, Amsterdam, The Netherlands.
Cancer Center Amsterdam, Biomarkers and Imaging, Amsterdam, the Netherlands.

Classifications MeSH