Evidence map›Paper›PMID 34641324›Full record

ArticleMolecules (Basel, Switzerland)2021

The Design, Synthesis, and Biological Activities of Pyrrole-Based Carboxamides: The Novel Tubulin Inhibitors Targeting the Colchicine-Binding Site.

Sergei Boichuk, Aigul Galembikova, Kirill Syuzov, Pavel Dunaev, Firuza Bikinieva, Aida Aukhadieva, Svetlana Zykova, Nazim Igidov, Ksenia Gankova, Maria Novikova and 1 more

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
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

7 citing papers in PubMed, 34 citations in OpenAlex.

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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

11 authors at 2 institutions in 1 country.

Sergei BoichukDepartment of Pathology, Kazan State Medical University, 420012 Kazan, Russia.ORCID 0000-0003-2415-1084
Aigul GalembikovaDepartment of Pathology, Kazan State Medical University, 420012 Kazan, Russia.ORCID 0000-0002-0293-2974
Kirill SyuzovDepartment of Pathology, Kazan State Medical University, 420012 Kazan, Russia.ORCID 0000-0003-3061-3150
Pavel DunaevDepartment of Pathology, Kazan State Medical University, 420012 Kazan, Russia.ORCID 0000-0002-5449-4435
Firuza BikinievaDepartment of Pathology, Kazan State Medical University, 420012 Kazan, Russia.ORCID 0000-0002-9012-6525
Aida AukhadievaDepartment of Pathology, Kazan State Medical University, 420012 Kazan, Russia.
Svetlana ZykovaPerm State Academy of Pharmacy, 614990 Perm, Russia.
Nazim IgidovPerm State Academy of Pharmacy, 614990 Perm, Russia.
Ksenia GankovaPerm State Academy of Pharmacy, 614990 Perm, Russia.
Maria NovikovaCytogenetics Laboratory, Carcinogenesis Institute, N.N. Blokhin National Medical Research Center of Oncology, 115478 Moscow, Russia.
Pavel KopninCytogenetics Laboratory, Carcinogenesis Institute, N.N. Blokhin National Medical Research Center of Oncology, 115478 Moscow, Russia.ORCID 0000-0002-2078-4274
Kazan State Medical University · RUMoscow Architectural Institute · RU

Funding

Russian Science Foundation 20-15-0001
6 · The paper itself

Abstract

Microtubule targeting agents (MTAs) that interfere with the dynamic state of the mitotic spindle are well-known and effective chemotherapeutic agents. These agents interrupt the microtubule network via polymerization or depolymerization, halting the cell cycle progression and leading to apoptosis. We report two novel pyrrole-based carboxamides (CAs) (CA-61 and -84) as the compounds exhibiting potent anti-cancer properties against a broad spectrum of epithelial cancer cell lines, including breast, lung, and prostate cancer. The anti-cancer activity of CAs is due to their ability to interfere with the microtubules network and inhibit tubulin polymerization. Molecular docking demonstrated an efficient binding between these ligands and the colchicine-binding site on the tubulin. CA-61 formed two hydrogen bond interactions with THR 179 (B) and THR 353 (B), whereas two hydrogen bonds with LYS 254 (B) and 1 with ASN 101 (A) were identified for CA-84. The binding energy for CA-84 and CA-61 was -9.910 kcal/mol and -9.390 kcal/mol. A tubulin polymerization assay revealed a strong inhibition of tubulin polymerization induced by CA-61 and -84. The immunofluorescence data revealed the disruption of the tubulin assembly in CA-treated cancer cells. As an outcome of the tubulin inhibition, these compounds halted the cell cycle progression in the G2/M phase, leading to the accumulation of the mitotic cells, and further induced apoptosis. Lastly, the in vivo study indicated that CAs significantly inhibited the HCC1806 breast cancer xenograft tumor growth in a nude mouse model. Collectively, we identified the novel CAs as potent MTAs, inhibiting tubulin polymerization via binding to the colchicine-binding site, disrupting the microtubule network, and exhibiting potent pro-apoptotic activities against the epithelial cancer cell lines both in vitro and in vivo.

Indexed as

AnimalsAntineoplastic AgentsBinding SitesBreast NeoplasmsCell Line, TumorCell ProliferationColchicineDrug DesignFemaleMiceMice, NudeMolecular ConformationMolecular Docking SimulationMolecular StructurePyrrolesStructure-Activity RelationshipAntineoplastic AgentsColchicinePyrrolesTubulin Modulators2-amino pyrrolesapoptosisbreastcell cyclelungmicrotubulesmitotic arrestpaclitaxelprostate cancertubulin depolymerizationvinblastine

Identifiers

PMID34641324
PMCPMC8510300
OpenAlexW3202442635

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.