Evidence map›Paper›PMID 37344820›Full record

ArticleCancer cell international2023

Antimicrobial peptide moricin induces ROS mediated caspase-dependent apoptosis in human triple-negative breast cancer via suppression of notch pathway.

Imran Ahmad, Saurabh Pal, Ranjana Singh, Khursheed Ahmad, Nilanjan Dey, Aditi Srivastava, Rumana Ahmad, Muath Suliman, Mohammad Y Alshahrani, Md Abul Barkat and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Cancer cell international, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

6 citing papers in PubMed, 10 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 5 institutions in 2 countries.

Imran Ahmad *Department of Biochemistry, King George's Medical University, Lucknow, 226003, India. imranahmadysbiochem@kgmcindia.edu.
Saurabh Pal *Department of Biotechnology, Era's Lucknow Medical College & Hospital, Era University, Lucknow, 226003, India.
Ranjana SinghDepartment of Biochemistry, King George's Medical University, Lucknow, 226003, India. ranjanasingh@kgmcindia.edu.
Khursheed AhmadDepartment of Biotechnology, Era's Lucknow Medical College & Hospital, Era University, Lucknow, 226003, India.
Nilanjan DeyDepartment of Chemistry, BITS- Pilani Hyderabad Campus, Hyderabad, 500078, Telangana, India.
Aditi SrivastavaDepartment of Biochemistry, Era's Lucknow Medical College & Hospital, Era University, Lucknow, 226003, India.
Rumana AhmadDepartment of Biochemistry, Era's Lucknow Medical College & Hospital, Era University, Lucknow, 226003, India.
Muath SulimanDepartment of Clinical Laboratory Sciences, College of Applied Medical Sciences, King Khalid University, Abha, Saudi Arabia.
Mohammad Y AlshahraniDepartment of Clinical Laboratory Sciences, College of Applied Medical Sciences, King Khalid University, Abha, Saudi Arabia.
Md Abul BarkatDepartment of Pharmaceutics, College of Pharmacy, University of Hafr Al-Batin, Al Jamiah, Hafr Al Batin, 39524, Saudi Arabia.
Sahabjada SiddiquiDepartment of Biotechnology, Era's Lucknow Medical College & Hospital, Era University, Lucknow, 226003, India. sahabjadabiotech04@gmail.com.
Era's Lucknow Medical College and Hospital · INKing George's Medical University · INKing Khalid University · SABirla Institute of Technology and Science - Hyderabad Campus · INUniversity of Hafr Al-Batin · SA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundBreast cancer is the world's most prevalent cancer among women. Microorganisms have been the richest source of antibiotics as well as anticancer drugs. Moricin peptides have shown antibacterial properties; however, the anticancer potential and mechanistic insights into moricin peptide-induced cancer cell death have not yet been explored.

methodsAn investigation through in silico analysis, analytical methods (Reverse Phase-High Performance Liquid Chromatography (RP-HPLC), mass spectroscopy (MS), circular dichroism (CD), and in vitro studies, has been carried out to delineate the mechanism(s) of moricin-induced cancer cell death. An in-silico analysis was performed to predict the anticancer potential of moricin in cancer cells using Anti CP and ACP servers based on a support vector machine (SVM). Molecular docking was performed to predict the binding interaction between moricin and peptide-related cancer signaling pathway(s) through the HawkDOCK web server. Further, in vitro anticancer activity of moricin was performed against MDA-MB-231 cells.

resultsIn silico observation revealed that moricin is a potential anticancer peptide, and protein-protein docking showed a strong binding interaction between moricin and signaling proteins. CD showed a predominant helical structure of moricin, and the MS result determined the observed molecular weight of moricin is 4544 Da. An in vitro study showed that moricin exposure to MDA-MB-231 cells caused dose dependent inhibition of cell viability with a high generation of reactive oxygen species (ROS). Molecular study revealed that moricin exposure caused downregulation in the expression of Notch-1, NF-ƙB and Bcl2 proteins while upregulating p53, Bax, caspase 3, and caspase 9, which results in caspase-dependent cell death in MDA-MB-231 cells.

conclusionsIn conclusion, this study reveals the anticancer potential and underlying mechanism of moricin peptide-induced cell death in triple negative cancer cells, which could be used in the development of an anticancer drug.

Indexed as

Anticancer peptideApoptosisMoricinNotch1Triple negative breast cancer

Identifiers

PMID37344820
PMCPMC10283202
OpenAlexW4381597437

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Registered trials

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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.