ArticleCancer cell international2005
Functional and structural characteristics of anticancer peptide Pep27 analogues.
Article in Cancer cell international, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 58 citations in OpenAlex.
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- Bacteriotherapy in Breast Cancer.International journal of molecular sciences · 2019Review
- A Synthetic Derivative of Antimicrobial Peptide Holothuroidin 2 from Mediterranean Sea Cucumber (Marine drugs · 2019Article
- Bacterial Proteinaceous Compounds With Multiple Activities Toward Cancers and Microbial Infection.Frontiers in microbiology · 2019Review
- Bacteria in Cancer Therapeutics: A Framework for Effective Therapeutic Bacterial Screening and Identification.Journal of Cancer · 2019Review
- Anticancer Activity of Bacterial Proteins and Peptides.Pharmaceutics · 2018Review
- Anticancer properties of a defensin like class IId bacteriocin Laterosporulin10.Scientific reports · 2017Article
- Spontaneous regression of tumour and the role of microbial infection--possibilities for cancer treatment.Anti-cancer drugs · 2016Review
- Discovery of Azurin-Like Anticancer Bacteriocins from Human Gut Microbiome through Homology Modeling and Molecular Docking against the Tumor Suppressor p53.BioMed research international · 2016Article
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Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA secreted peptide Pep27 initiates the cell death program in S. pneumoniae through signal transduction. This study was undertaken to evaluate the relation between the structure and cytotoxic activity of Pep27 and its analogues on cancer cells.
resultsPep27anal2 characterized substituting (2R-->W), (4E-->W), (11S-->W) and (13Q-->W) in native Pep27, exhibited greater hydrophobicity and anticancer activity than Pep27 and other analogues. The IC50 values of Pep27anal2 were approximately 10 - 30 microM in a number of cell lines (AML-2, HL-60, Jurkat, MCF-7 and SNU-601). Confocal microscopy showed that Pep27anal2-FITC was localized in the plasma membrane, and then moving from the membrane to subcellular compartments with the initiation of membrane blebbing. Flow cytometric analysis using propidium iodide and Annexin V also revealed that Pep27anal2 induced apoptosis with minor membrane damage. Electron microscopy revealed that Pep27 induced apoptosis in Jurkat cells. The anticancer activity of Pep27anal2 was neither abrogated by pan-caspase inhibitor (Z-VAD-fmk) nor related to cytochrome c release from mitochondria. The 3D solution structures of these two Pep27 peptides revealed that both form a random coil conformation in water; however, they adopted stable alpha-helical conformations in solutions.
conclusionThe results indicate that Pep27anal2 can penetrate the plasma membrane, and then induce apoptosis in both caspase-and cytochrome c-independent manner. The hydrophobicity of Pep27anal2 appears to play an important role in membrane permeabilization and/or anticancer properties. The structure-functional relationships of these peptides are also discussed. It is proposed that Pep27anal2 is a potential candidate for anticancer therapeutic agents.
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Registered trials
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