Evidence map›Paper›PMID 32229347›Full record

ArticleBioorganic chemistry2020

Development and biological investigations of hypoxia-sensitive prodrugs of the tyrosine kinase inhibitor crizotinib.

Bjoern Bielec, Hemma Schueffl, Alessio Terenzi, Walter Berger, Petra Heffeter, Bernhard K Keppler, Christian R Kowol

Abstract read
In one paragraph

Article in Bioorganic chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

10 citing papers in PubMed.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Nitroaromatic Hypoxia-Activated Prodrugs for Cancer Therapy.Pharmaceuticals (Basel, Switzerland) · 2022
    Review
  6. Therapeutic targeting of the hypoxic tumour microenvironment.Nature reviews. Clinical oncology · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Bjoern BielecInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Strasse 42, 1090 Vienna, Austria.
Hemma SchuefflInstitute of Cancer Research, Medical University of Vienna, Borschkegasse 8a, 1090 Vienna, Austria.
Alessio TerenziDonostia International Physics Center, Paseo Manuel de Lardizabal 4, Donostia 20018, Spain.
Walter BergerInstitute of Cancer Research, Medical University of Vienna, Borschkegasse 8a, 1090 Vienna, Austria; Research Cluster ''Translational Cancer Therapy Research'', Vienna, Austria.
Petra HeffeterInstitute of Cancer Research, Medical University of Vienna, Borschkegasse 8a, 1090 Vienna, Austria; Research Cluster ''Translational Cancer Therapy Research'', Vienna, Austria. Electronic address: petra.heffeter@meduniwien.ac.at.
Bernhard K KepplerInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Strasse 42, 1090 Vienna, Austria; Research Cluster ''Translational Cancer Therapy Research'', Vienna, Austria.
Christian R KowolInstitute of Inorganic Chemistry, Faculty of Chemistry, University of Vienna, Waehringer Strasse 42, 1090 Vienna, Austria; Research Cluster ''Translational Cancer Therapy Research'', Vienna, Austria. Electronic address: christian.kowol@univie.ac.at.

Funding

Austrian Science Fund FWF P 28853
6 · The paper itself

Abstract

Despite the huge success of tyrosine kinase inhibitors as anticancer agents, severe side effects are a major problem. In order to overcome this drawback, the first hypoxia-activatable 2-nitroimidazole-based prodrugs of the clinically approved ALK and c-MET inhibitor crizotinib were developed. The 2-aminopyridine functionality of crizotinib (essential for target kinase binding) was considered as ideal position for prodrug derivatization. Consequently, two different prodrugs were synthesized with the nitroimidazole unit attached to crizotinib either via carbamoylation (A) or alkylation (B) of the 2-aminopyridine moiety. The successful prodrug design could be proven by docking studies and a dramatically reduced ALK and c-MET kinase-inhibitory potential. Furthermore, the prodrugs showed high stability in serum and release of crizotinib in an enzymatic nitroreductase-based cleavage assay was observed for prodrug A. The in vitro activity of both prodrugs was investigated against ALK- and c-MET-dependent or -overexpressing cells, revealing a distinct hypoxia-dependent activation for prodrug A. Finally, inhibition of c-MET phosphorylation and cell proliferation could also be proven in vivo. In summary of the theoretical, chemical and biological studies, prodrug derivatization of the 2-aminopyridine position can be considered as a promising strategy to reduce the side effects and improve the anticancer activity of crizotinib.

Indexed as

Drug DevelopmentAnaplastic Lymphoma KinaseAntineoplastic AgentsCell HypoxiaCell ProliferationCells, CulturedCrizotinibDose-Response Relationship, DrugDrug Screening Assays, AntitumorHumansMolecular StructureProdrugsProtein Kinase InhibitorsProto-Oncogene Proteins c-metStructure-Activity RelationshipALK protein, humanAnaplastic Lymphoma KinaseAntineoplastic AgentsCrizotinibProdrugsProtein Kinase InhibitorsProto-Oncogene Proteins c-metCrizotinibHypoxiaNitroimidazoleProdrugsTyrosine kinase inhibitor

Identifiers

PMID32229347
PMCPMC7611434

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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.