The synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells

dc.creatorAbdel-Salam, Mostafa A. L.
dc.creatorCarvalho-Tavares, Juliana
dc.creatorGomes, Kamila Sousa
dc.creatorCarvalho, Andrea Teixeira de
dc.creatorKitten, Gregory T.
dc.creatorNyffeler, Johanna
dc.creatorDias, Felipe F.
dc.creatorReis, Pablo V. Mendes dos
dc.creatorPimenta, Adriano M. C.
dc.creatorLeist, Marcel
dc.creatorLima, Maria Elena de
dc.creatorSouza-Fagundes, Elaine Maria de
dc.date2019-11-20T17:20:14Z
dc.date2019-11-20T17:20:14Z
dc.date2019
dc.date.accessioned2023-09-26T20:22:16Z
dc.date.available2023-09-26T20:22:16Z
dc.identifierABDEL-SALAM, Mostafa A. L. et al. The synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells. Amino Acids, v. 51, n. 3, p. 433-449 2019.
dc.identifier0939-4451
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/37205
dc.identifier10.1007/s00726-018-2678-4
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8855364
dc.descriptionAntimicrobial peptides present a broad spectrum of therapeutic applications, including their use as anticancer peptides. These peptides have as target microbial, normal, and cancerous cells. The oncological properties of these peptides may occur by membranolytic mechanisms or non-membranolytics. In this work, we demonstrate for the first time the cytotoxic effects of the cationic alpha-helical antimicrobial peptide LyeTx I-b on glioblastoma lineage U87-MG. The anticancer property of this peptide was associated with a membranolytic mechanism. Loss of membrane integrity occurred after incubation with the peptide for 15 min, as shown by trypan blue uptake, reduction of calcein-AM conversion, and LDH release. Morphological studies using scanning electron microscopy demonstrated disruption of the plasma membrane from cells treated with LyeTx I-b, including the formation of holes or pores. Transmission electron microscopy analyses showed swollen nuclei with mild DNA condensation, cell volume increase with an electron-lucent cytoplasm and organelle vacuolization, but without the rupture of nuclear or plasmatic membranes. Morphometric analyses revealed a high percentage of cells in necroptosis stages, followed by necrosis and apoptosis at lower levels. Necrostatin-1, a known inhibitor of necroptosis, partially protected the cells from the toxicity of the peptide in a concentration-dependent manner. Imaging flow cytometry confirmed that 59% of the cells underwent necroptosis after 3-h incubation with the peptide. It is noteworthy that LyeTx I-b showed only mild cytotoxicity against normal fibroblasts of human and monkey cell lines and low hemolytic activity in human erythrocytes. All data together point out the anticancer potential of this peptide.
dc.description2040-01-01
dc.formatapplication/pdf
dc.languageeng
dc.publisherSpringer-Verlag
dc.rightsrestricted access
dc.subjectAnticancer peptide
dc.subjectGlioblastoma multiform
dc.subjectLyeTx I-b
dc.subjectU-87 MG cells
dc.titleThe synthetic peptide LyeTxI-b derived from Lycosa erythrognatha spider venom is cytotoxic to U-87 MG glioblastoma cells
dc.typeArticle


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