Study of domains formation in model membranes induced by antimicrobial peptides and their action interfacial

• Grant number: 12/08147-8
• Support Opportunities: Scholarships in Brazil - Doctorate
• Start date: August 01, 2012
• End date: December 31, 2015
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: João Ruggiero Neto
• Grantee: Dayane dos Santos Alvares
• 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
• Associated scholarship(s): 15/01508-3 - Interaction of the antimicrobial and antitumor peptide, Polybia-MP1, with lipid-domains, BE.EP.DR

Abstract

Studies of correlations between structural aspects of lytic peptides, mastoparanos the family, and their lytic activity in model membranes, and antimicrobial activities performed by different experimental approaches, showed different mechanism of action for the same peptide depending on the ratio peptide/lipid. These studies revealed that a number of mastoparanos extracted from native wasps has interfacial activity and provided evidence that some of these peptides induce the formation of domains or segregation in lipid vesicles, which could constitute a alternate lytic mechanism for interfacial activity. The purpose of this project is to probe the studies of interfacial activity and formation of lipid domains using the techniques of differential scanning calorimetry (DSC), experiments on single vesicles (GUVs) visualized by fluorescence microscopy and phase contrast and technique monolayers lipid. The strategy is to use different systems miscible lipid mixtures which mimic membrane of gram negative bacteria and study phase transition from gel - liquid-crystal systems of these peptides in the presence of observing shifts in the thermograms and use GUVs to visualize of possible domains. In experiments with monolayers are obtained important information, such as penetration of peptides into monolayers and peptide-induced changes in the phase transition between liquid expanded - liquid condensed.

Scientific publications

(6)

(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)

PUIA ZANIN, LUCIANA MORO; ALVARES, DAYANE DOS SANTOS; JULIANO, MARIA APARECIDA; PAZIN, WALLANCE MOREIRA; ITO, AMANDO SIUITI; RUGGIERO NETO, JOO. Interaction of a synthetic antimicrobial peptide with model membrane by fluorescence spectroscopy. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, v. 42, n. 11-12, p. 819-831, DEC 2013. (12/08147-8, 11/11640-5)

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.; LAURA FANANI, MARIA; RUGGIERO NETO, JOAO; WILKE, NATALIA. The interfacial properties of the peptide Polybia-MP1 and its interaction with DPPC are modulated by lateral electrostatic attractions. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1858, n. 2, p. 393-402, FEB 2016. (12/08147-8, 11/11640-5)

LEITE, NATALIA BUENO; ALVARES, DAYANE DOS SANTOS; DE SOUZA, BIBIANA MONSON; PALMA, MARIO SERGIO; RUGGIERO NETO, JOAO. Effect of the aspartic acid D2 on the affinity of Polybia-MP1 to anionic lipid vesicles. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, v. 43, n. 4-5, p. 121-130, MAY 2014. (12/08147-8, 11/11640-5)

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)

Academic Publications

(References retrieved automatically from State of São Paulo Research Institutions)

ALVARES, Dayane dos Santos. Study of domains formation in model membranes induced by antimicrobial peptides and their interfacial action. 2016. Doctoral Thesis - Universidade Estadual Paulista (Unesp). Instituto de Biociências Letras e Ciências Exatas. São José do Rio Preto São José do Rio Preto.