Selective cytotoxic effect against the MDA-MB-468 breast cancer cell line of the antibacterial palindromic peptide derived from bovine lactoferricin

Barragán‐Cárdenas, Andrea Carolina; Urrea-Pelayo, Maribel; Niño‐Ramírez, Victor Alfonso; Umaña‐Pérez, Adriana; Vernot, Jean-Paul; Parra-Giraldo, Claudia Marcela; Fierro-Medina, Ricardo; Rivera‐Monroy, Zuly Jenny; García‐Castañeda, Javier Eduardo

doi:10.1039/d0ra02688c

Cited by 17 publications

(30 citation statements)

References 48 publications

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“…At 6.25 μM, it showed 80 % viability but at the maximum concentration tested the cell viability decreased to 10 %. It is already reported that Brevinin‐1BYa peptides inhibit the growth of cancer cells such as MDA‐MB‐231 breast carcinoma and HepG2 hepatoma‐derived cells [29] . A likely explanation for the selective action of the peptide against cancer cells over normal cells is that negative charges on the membrane components in cancer cells such as phosphatidylserine, glycosylated mucins, sialylated gangliosides, and sialic acid interact with positively‐charged peptides [30] .…”

Section: Resultsmentioning

confidence: 99%

“…According to the World Health Organization, the incidence and mortality rate of breast cancer is estimated to be among the highest in the world, with an estimated 2.26 million new diagnoses and approximately 685 000 deaths in 2020 [28] . It is imperative to develop novel anti‐cancer therapies due to the toxicity associated with many conventional chemotherapeutic agents, as well as the development of chemotherapy resistance [29] . In order to improve treatment, antimicrobial peptides (AMPs) are being studied as potential therapeutic agents.…”

Section: Resultsmentioning

confidence: 99%

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Membrane Disruptive Action of Cationic Antibacterial Peptide B1CTcu3

et al. 2022

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A twenty-two-residue peptide Brevinin1 Clinotarsus curtipus-3 (B1CTcu3), identified from the skin secretion of frog Clinotarsus curtipes of the Western Ghats, exhibited a broad range of antibacterial activity against Gram-negative and Gram-positive bacteria, including the methicillin-resistant Staphylococcus aureus (MRSA). It showed anti-biofilm activity even at subminimum inhibitory concentration (sub-MIC) against Pseudomonas aeruginosa and Staphylococcus aureus. Analysis of the scanning electron microscopic (SEM) images, confocal images, flow cytometric data and the effect of salt concentration on antibacterial potency suggests that the killing action of the peptide is through the membranolytic process. Single channel electric recording confirmed that the peptide elicited pores on the bacterial cell membrane as it induces a heterogeneous channel in the lipid bilayer. It also showed cytotoxicity against MDA-MB-231 breast cancer cell with IC 50 of 25 μM. B1CTcu3 peptide could serve as the template for next-generation antibacterial agents, particularly against antibiotic resistant pathogenic bacteria.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Membrane Disruptive Action of Cationic Antibacterial Peptide B1CTcu3

et al. 2022

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“…The peptide used in this study was synthesized with low purity. However, there are several studies using peptides with 10% impurity or higher to assess the functional assay, and results could provide appropriate information of the cytotoxicity [23,24]. In addition, novel peptide of pathogenic L. interrogans exhibited a cytotoxic effect against a monkey kidney Vero cell line in a dose-dependent manner.…”

Section: Discussionmentioning

confidence: 99%

“…The amino acid sequence of the novel peptide based on sequence alignment to the MASCOT database was synthesized with 90.78% purity (KareBay Biochem, Inc., South Brunswick Township, NJ, USA) [23,24]. The secondary structure of the synthetic peptide was analyzed by circular dichroism (CD) spectroscopy.…”

Section: Characterization Of the Novel Peptide Sequencementioning

confidence: 99%

Characterization of a Novel Peptide from Pathogenic Leptospira and Its Cytotoxic Effect

et al. 2020

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Leptospirosis is a zoonotic infectious disease caused by pathogenic Leptospira species. Virulence proteins have been shown to be key determinants of the pathogenesis of pathogenic Leptospira. A specific peptide at a mass-to-charge ratio of 7000 Da was identified in Leptospira whole cells using matrix-assisted laser/desorption ionization time-of-flight (MALDI-TOF) mass spectrometry. This peptide was specifically present in pathogenic Leptospira and in clinical isolates. We report here the characterization of this specific peptide using a proteomics approach. This peptide was significantly matched to a hypothetical conserved L. interrogans protein (LA2458) with a calculated molecular weight of 7140.136 Da containing a tellurite-resistance domain at its C terminus (TerB-C). The amino acid sequences revealed the presence of hydrophobic transmembrane portions and two linear B-cell epitopes. Despite its low abundance, this synthetic peptide demonstrated dose-dependent cytotoxicity toward African green monkey kidney (Vero) cells via the apoptosis pathway. The concentration of the peptide 100 µM induced about 50% of cell death after a 24 h exposure. This peptide could be useful for the diagnosis of leptospirosis and the study of pathogenesis.

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“…This peptide did not generate a cytotoxic effect on fibroblasts, suggesting that it exhibits selectivity for cancer cells. [40] In the present paper, we explored the peptide synthesis scaling following the Good Manufacture Practice (GMP) guidelines [41] for the palindromic peptide LfcinB (21-25) Pal : 1 RWQWRWQWR 9 . Also its cytotoxic effect was evaluated against human cell lines derived from breast cancer cells MDA-MB-231 and MCF-7, in addition to its selectivity against non-cancerous cells MCF-12, BMEC, and primary fibroblast culture.…”

Section: Introductionmentioning

confidence: 99%

The Nonapeptide RWQWRWQWR: A Promising Molecule for Breast Cancer Therapy

et al. 2020

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The palindromic nonapeptide H‐1RWQWRWQWR9‐NH2 (LfcinB (21–25)Pal) was synthetize and scaled following the good manufacturing practices (GMP) guidelines to obtained batches up to 1 g of pure peptide which evidencing their synthetic viability. Its cytotoxic effect was tested against breast cancer cell lines MDA‐MB‐231 and MCF‐7 and was dependent on concentration against both. The IC50 values were 135 μM and 66 μM, respectively. Against MCF‐7 the peptide exerts its greater cytotoxic effect at 135 μM, diminishing their cell viability to 21%. Furthermore, the palindromic peptide did not exhibit a significant cytotoxic effect against the nontumorigenic cells MCF‐12, BMEC (bovine mammary epithelial cells) or fibroblast, which confirms its selectivity. The cancerous cells treated at 135 μM for 2 h exhibited morphological changes like cellular shrinkage and rounded forms. Trough flow cytometry assays we evidence that 73% of the events were related to late apoptosis, and cells that exhibited mitochondrial membrane depolarization also had an increase in the relative expression of caspase‐3. Our results suggest that the LfcinB (21–25)Pal peptide has a cytotoxic effect against MCF‐7 mainly through apoptotic events which makes it a promising candidate for therapeutic agent.

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Selective cytotoxic effect against the MDA-MB-468 breast cancer cell line of the antibacterial palindromic peptide derived from bovine lactoferricin

Abstract: The cytotoxic effect against the breast cancer cell line MDA-MB-468 of the palindromic peptide LfcinB (21–25)Pal: 1RWQWRWQWR9 and its analogous peptides, obtained via alanine scanning, was evaluated.

Cited by 17 publications

References 48 publications

Membrane Disruptive Action of Cationic Antibacterial Peptide B1CTcu3

Membrane Disruptive Action of Cationic Antibacterial Peptide B1CTcu3

Characterization of a Novel Peptide from Pathogenic Leptospira and Its Cytotoxic Effect

The Nonapeptide RWQWRWQWR: A Promising Molecule for Breast Cancer Therapy

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