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Interaction membrane/peptide: mechanical and electrostatic properties in system with lipid domains

Grant number: 15/25620-7
Support type:Scholarships in Brazil - Post-Doctorate
Effective date (Start): February 01, 2017
Effective date (End): March 31, 2021
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Cooperation agreement: Coordination of Improvement of Higher Education Personnel (CAPES)
Principal Investigator:João Ruggiero Neto
Grantee:Dayane dos Santos Alvares
Home 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):18/14215-2 - Regulation of the activity of antimicrobial peptides by the mechanical properties of the host membrane, BE.EP.PD

Abstract

Polybia-MP1, extracted from the venom of a Brazilian wasp Polybia paulista, is highly active on the anionic lipid membrane surface displaying antimicrobial and anticancer activities. Our hypothesis is that changes that occur on the surface of apoptotic cell, as compressibility, elasticity, fluidity modulated by different lipid composition, are the key to a selectivity of Polybia-MP1 to these cells. The association of this peptide to membrane affects strongly the structural and dynamics properties of lipids, disturbing the lipid packing. We gathered strong experimental evidences that revealed the complex connection between electrostatic, hydrophobic and elastic phenomena occurring at the interface water-membrane. From the Biophysical point of view, understanding the physical-chemical properties of the interaction peptide/membrane in the interface investigating mechanical factors that affect the selectivity of this peptide, is a major scientific challenge and is the main purpose of this work. The strategy is to use different experimental techniques as differential scanning calorimetry (DSC), visualization of giant vesicles (GUVs) by phase contrast and fluorescence and fluorescence confocal microscopies, associated to monolayers technique at the air-water interface, to study and characterize in detail the changes that occur in lipids (elastic and segregation effects) caused by the interaction with peptides. We expect to get details to help understanding the selectivity in the action of bioactive peptides. (AU)

Scientific publications (5)
(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)
MIASAKI, KENNETH M. F.; WILKE, NATALIA; RUGGIERO NETO, JOAO; ALVARES, DAYANE S. N-terminal acetylation of a mastoparan-like peptide enhances PE/PG segregation in model membranes. Chemistry and Physics of Lipids, v. 232, OCT 2020. Web of Science Citations: 0.
ALVARES, DAYANE S.; VIEGAS, TAISA G.; NETO, JOAO RUGGIERO. The effect of pH on the lytic activity of a synthetic mastoparan-like peptide in anionic model membranes. Chemistry and Physics of Lipids, v. 216, p. 54-64, NOV 2018. Web of Science Citations: 1.
ALVARES, DAYANE S.; WILKE, NATALIA; RUGGIERO NETO, JOAO. Effect of N-terminal acetylation on lytic activity and lipid-packing perturbation induced in model membranes by a mastoparan-like peptide. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1860, n. 3, p. 737-748, MAR 2018. Web of Science Citations: 2.
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. Web of Science Citations: 8.
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. Web of Science Citations: 4.

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