Interaction of the antimicrobial and antitumor peptide, Polybia-MP1, with lipid-domains

• Grant number: 15/01508-3
• Support Opportunities: Scholarships abroad - Research Internship - Doctorate
• Start date: April 30, 2015
• End date: August 29, 2015
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: João Ruggiero Neto
• Grantee: Dayane dos Santos Alvares
• Supervisor: María Laura Fanani
• Host Institution: Instituto de Biociências, Letras e Ciências Exatas (IBILCE). Universidade Estadual Paulista (UNESP). Campus de São José do Rio Preto. São José do Rio Preto , SP, Brazil
• Institution abroad: Universidad Nacional de Córdoba (UNC), Argentina
• Associated to the scholarship: 12/08147-8 - Study of domains formation in model membranes induced by antimicrobial peptides and their action interfacial, BP.DR

Abstract

A growing number of studies have shown that some of the cationic antimicrobial peptides (AMPs) have a broad spectrum of cytotoxic activity against cancer cells. The antimicrobial tetradecapeptide Polybia-MP1, extracted from a native wasp, exhibits antitumor activity on prostate and bladder cancer cell cultures and high specificity to leukemic T-lymphocyte. Its inhibitory effect on cancer cell proliferation is believed to be due to the presence of both phosphatidylserine (PS) and phosphatidylethanolamine (PE) lipids in the outer membrane leaflet of these cells. The MP1 interaction with anionic vesicles suggested interfacial action inducing lipid segregation or domain formation. Then, the inducing of lateral phase separation can be the mechanism involved in the anticancer activity of MP1. The proposal of this work is to investigate the effect of MP1 when interacting with membrane systems that present lipid domains. In addition, it will be investigated whether the peptide is also able to induce membrane-domain segregation when is associated with the lipid interface. These studies will be performed with state-of the art techniques such as Brewster angle (BAM) and confocal-fluorescence microscopies. With BAM, the effect of MP1 on the phase-behavior of lipid Langmuir monolayer will be observed. With the use of confocal-fluorescence microscopy, now the lytic action of the MP1 will be investigated when interacts with giant unilamellar vesicles (GUVs) of different lipid composition. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

ALVARES, DAYANE S.; RUGGIERO NETO, JOAO; AMBROGGIO, ERNESTO E.. Phosphatidylserine lipids and membrane order precisely regulate the activity of Polybia-MP1 peptide. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1859, n. 6, p. 1067-1074, JUN 2017. (12/08147-8, 15/25619-9, 11/11640-5, 15/25620-7, 11/51684-1, 15/01508-3)

ALVARES, DAYANE S.; WILKE, NATALIA; RUGGIERO NETO, JOAO; FANANI, MARIA LAURA. The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state. Chemistry and Physics of Lipids, v. 207, n. A, p. 38-48, OCT 2017. (11/51684-1, 12/08147-8, 11/11640-5, 15/25619-9, 15/01508-3, 15/25620-7)

ALVARES, DAYANE S.; WILKE, NATALIA; RUGGIERO NETO, JOAO; FANANI, MARIA LAURA. The insertion of Polybia-MP1 peptide into phospholipid monolayers is regulated by its anionic nature and phase state. Chemistry and Physics of Lipids, v. 207, p. 11-pg., 2017-10-01. (15/25620-7, 12/08147-8, 11/11640-5, 11/51684-1, 15/01508-3, 15/25619-9)