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Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III
Biological activity of the new antimicrobial peptide polyphemusin III from the horseshoe crab Limulus polyphemus was examined against bacterial strains and human cancer, transformed, and normal cell cultures. Polyphemusin III has the amino acid sequence RRGCFRVCYRGFCFQRCR and is homologous to other...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315362/ https://www.ncbi.nlm.nih.gov/pubmed/30486233 http://dx.doi.org/10.3390/md16120466 |
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author | Marggraf, Mariana B. Panteleev, Pavel V. Emelianova, Anna A. Sorokin, Maxim I. Bolosov, Ilia A. Buzdin, Anton A. Kuzmin, Denis V. Ovchinnikova, Tatiana V. |
author_facet | Marggraf, Mariana B. Panteleev, Pavel V. Emelianova, Anna A. Sorokin, Maxim I. Bolosov, Ilia A. Buzdin, Anton A. Kuzmin, Denis V. Ovchinnikova, Tatiana V. |
author_sort | Marggraf, Mariana B. |
collection | PubMed |
description | Biological activity of the new antimicrobial peptide polyphemusin III from the horseshoe crab Limulus polyphemus was examined against bacterial strains and human cancer, transformed, and normal cell cultures. Polyphemusin III has the amino acid sequence RRGCFRVCYRGFCFQRCR and is homologous to other β-hairpin peptides from the horseshoe crab. Antimicrobial activity of the peptide was evaluated and MIC (minimal inhibitory concentration) values were determined. IC(50) (half-maximal inhibitory concentration) values measured toward human cells revealed that polyphemusin III showed a potent cytotoxic activity at concentrations of <10 μM. Polyphemusin III caused fast permeabilization of the cytoplasmic membrane of human leukemia cells HL-60, which was measured with trypan blue exclusion assay and lactate dehydrogenase-release assay. Flow cytometry experiments for annexin V-FITC/ propidium iodide double staining revealed that the caspase inhibitor, Z-VAD-FMK, did not abrogate disruption of the plasma membrane by polyphemusin III. Our data suggest that polyphemusin III disrupts the plasma membrane integrity and induces cell death that is apparently not related to apoptosis. In comparison to known polyphemusins and tachyplesins, polyphemusin III demonstrates a similar or lower antimicrobial effect, but significantly higher cytotoxicity against human cancer and transformed cells in vitro. |
format | Online Article Text |
id | pubmed-6315362 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-63153622019-01-10 Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III Marggraf, Mariana B. Panteleev, Pavel V. Emelianova, Anna A. Sorokin, Maxim I. Bolosov, Ilia A. Buzdin, Anton A. Kuzmin, Denis V. Ovchinnikova, Tatiana V. Mar Drugs Article Biological activity of the new antimicrobial peptide polyphemusin III from the horseshoe crab Limulus polyphemus was examined against bacterial strains and human cancer, transformed, and normal cell cultures. Polyphemusin III has the amino acid sequence RRGCFRVCYRGFCFQRCR and is homologous to other β-hairpin peptides from the horseshoe crab. Antimicrobial activity of the peptide was evaluated and MIC (minimal inhibitory concentration) values were determined. IC(50) (half-maximal inhibitory concentration) values measured toward human cells revealed that polyphemusin III showed a potent cytotoxic activity at concentrations of <10 μM. Polyphemusin III caused fast permeabilization of the cytoplasmic membrane of human leukemia cells HL-60, which was measured with trypan blue exclusion assay and lactate dehydrogenase-release assay. Flow cytometry experiments for annexin V-FITC/ propidium iodide double staining revealed that the caspase inhibitor, Z-VAD-FMK, did not abrogate disruption of the plasma membrane by polyphemusin III. Our data suggest that polyphemusin III disrupts the plasma membrane integrity and induces cell death that is apparently not related to apoptosis. In comparison to known polyphemusins and tachyplesins, polyphemusin III demonstrates a similar or lower antimicrobial effect, but significantly higher cytotoxicity against human cancer and transformed cells in vitro. MDPI 2018-11-26 /pmc/articles/PMC6315362/ /pubmed/30486233 http://dx.doi.org/10.3390/md16120466 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Marggraf, Mariana B. Panteleev, Pavel V. Emelianova, Anna A. Sorokin, Maxim I. Bolosov, Ilia A. Buzdin, Anton A. Kuzmin, Denis V. Ovchinnikova, Tatiana V. Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III |
title | Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III |
title_full | Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III |
title_fullStr | Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III |
title_full_unstemmed | Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III |
title_short | Cytotoxic Potential of the Novel Horseshoe Crab Peptide Polyphemusin III |
title_sort | cytotoxic potential of the novel horseshoe crab peptide polyphemusin iii |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6315362/ https://www.ncbi.nlm.nih.gov/pubmed/30486233 http://dx.doi.org/10.3390/md16120466 |
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