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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

Biophysical characterization and antitumor activity of synthetic Pantinin peptides from scorpion's venom

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Author(s):
Crusca, Jr., Edson [1] ; Mansor Basso, Luis Guilherme [2] ; Altei, Wanessa Fernanda [3] ; Marchetto, Reinaldo [1]
Total Authors: 4
Affiliation:
[1] Sao Paulo State Univ, UNESP, Dept Biochem & Technol Chem, Inst Chem, Araraquara, SP - Brazil
[2] Univ Sao Paulo, Sch Philosophy Sci & Letters Ribeirao Preto, Phys Dept, Mol Biophys Lab, Av Bandeirantes 3900, BR-14040901 Ribeirao Preto - Brazil
[3] Univ Fed Sao Carlos, Dept Physiol Sci, Lab Biochem & Mol Biol, Sao Carlos, SP - Brazil
Total Affiliations: 3
Document type: Journal article
Source: BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES; v. 1860, n. 11, p. 2155-2165, NOV 2018.
Web of Science Citations: 2
Abstract

Antimicrobial peptides have been extensively described as bioactive agents, mainly considering their selective toxicity towards bacteria but not to healthy mammalian cells. In past years, this class of compounds has been classified as an attractive and novel family of anticancer agents. Pantinin peptides isolated from scorpion Pandinus imperator presented antimicrobial activity. In this study, we have explored the in vitro antitumor activity of antimicrobial pantinin peptides against the tumor cell lines MDA-MB-231 (breast adenocarcinoma) and DU - 145 (prostate adenocarcinoma) and healthy fibroblasts HGF - 1. To further improve our mechanistic understanding for this class of compounds, we have also performed a biophysical characterization of these peptides in lipid model membranes. Cell viability assays revealed that all peptides were more effective on tumor cells when compared to fibroblasts, indicating selectivity towards cancer cells. Furthermore, flow cytometry analysis revealed that all peptides induced apoptosis in cancer cells in a different way from fibroblasts. Circular dichroism spectroscopy showed that all peptides adopted an alpha-helical structure and an evaluation of the binding constant indicates a higher affinity of the peptides to negatively charged phospholipids. Additionally, permeabilization assays showed that POPG and POPS anionic vesicles were more susceptible to peptide-induced lysis than POPC:Chol and POPC:POPE vesicles. Moreover, we have observed that increasing concentrations of cholesterol inhibits peptide binding process. Therefore, our findings suggest that Pantinin peptides may have chemotherapeutic potential for cancer treatment. (AU)

FAPESP's process: 14/18747-8 - Tumor breast cell exosomes and their role in cell adhesion during metastasis
Grantee:Wanessa Fernanda Altei
Support Opportunities: Scholarships in Brazil - Post-Doctoral
FAPESP's process: 14/00206-0 - Structure and function of SARS-CoV spike glycoprotein fusion peptides
Grantee:Luís Guilherme Mansor Basso
Support Opportunities: Scholarships in Brazil - Post-Doctoral