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Effect of aminophospholipids and of the pH on the interfacial activity of the anticancer peptide Polybia-MP1 and analogs in model membranes

Grant number:15/25619-9
Support Opportunities:Regular Research Grants
Start date: March 01, 2016
End date: February 28, 2019
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Principal Investigator:João Ruggiero Neto
Grantee:João Ruggiero Neto
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
City of the host institution:São José do Rio Preto

Abstract

The antimicrobial peptide Polybia-MP1 (MP1) extracted from the native wasp Polybia paulista, revealed to be inhibitor of cancer cell proliferation besides its potent antibacterial activity. It selectively recognized leukemic T-limphocytes but not the health ones, displaying thus a potential for pharmaceutical and medical applications. We gathered strong experimental evidences indicating that the origin of this activity and selectivity is the presence of aminophospholipids phosphatidylserine (PS) and phosphatidylethanolamine (PE) in the outer leaflet of these cells. PS and PE act synergistically, PS is anionic and enhances the cationic peptide affinity and PE increases in one magnitude order the membrane permeability induced by the peptide. We have also observed that for peptides with acidic and basic residues the affinity to anionic membranes is modulated by the pH. The purpose of the present project is to investigate the biophysical-chemical bases of the synergy between PS and PE as well as the effect of small pH changes that characterize the extracellular milieu of these cells. The main focus is to understand the aspects involved in the adsorption of the peptide to the lipid bilayer and its effects on the lipid packing and on the lytic activity, and still the influences of the pH. The purpose is to use different experimental approaches that contribute to explore the synergy of these lipids and to design sequences responsive to the pH changes in the same range observed between physiologic and extracellular milieu. Hopefully, the results to be obtained will certainly contribute to the comprehension of important aspects at the interface that modulate the selectivity of these peptides contributing to the design of more selective sequences for medical applications. (AU)

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Scientific publications (9)
(The scientific publications listed on this page originate from the Web of Science or SciELO databases. Their authors have cited FAPESP grant or fellowship project numbers awarded to Principal Investigators or Fellowship Recipients, whether or not they are among the authors. This information is collected automatically and retrieved directly from those bibliometric databases.)
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, . (15/25620-7, 15/25619-9)
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, . (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. 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, . (15/25619-9, 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, n. A, p. 38-48, . (11/51684-1, 12/08147-8, 11/11640-5, 15/25619-9, 15/01508-3, 15/25620-7)
SANTANA MARTINS, INGRID BERNARDES; VIEGAS, TAISA GIORDANO; ALVARES, DAYANE DOS SANTOS; DE SOUZA, BIBIANA MONSON; PALMA, MARIO SERGIO; NETO, JOAO RUGGIERO; DE ARAUJO, ALEXANDRE SUMAN. The effect of acidic pH on the adsorption and lytic activity of the peptides Polybia-MP1 and its histidine-containing analog in anionic lipid membrane: a biophysical study by molecular dynamics and spectroscopy. Amino Acids, v. 53, n. 5, p. 753-767, . (15/25619-9, 16/16212-5, 15/25620-7, 10/18169-3)
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, . (15/25619-9, 15/25620-7)
ALVARES, DAYANE S.; MONTI, MARIELA R.; NETO, JOAO RUGGIERO; WILKE, NATALIA. The antimicrobial peptide Polybia-MP1 differentiates membranes with the hopanoid, diplopterol from those with cholesterol. BBA ADVANCES, v. 1, p. 11-pg., . (15/25619-9, 15/25620-7, 18/14215-2)
ALVARES, DAYANE DOS SANTOS; MARTINS, INGRID BERNARDES SANTANA; VIEGAS, TAISA GIORDANO; PALMA, MARIO SERGIO; DE ARAUJO, ALEXANDRE SUMAN; DE CARVALHO, SIDNEY JURADO; RUGGIERO NETO, JOAO. Modulatory Effects of Acidic pH and Membrane Potential on the Adsorption of pH-Sensitive Peptides to Anionic Lipid Membrane. MEMBRANES, v. 11, n. 5, p. 16-pg., . (15/25620-7, 10/18169-3, 16/16212-5, 18/01841-2, 15/25619-9)
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., . (15/25620-7, 12/08147-8, 11/11640-5, 11/51684-1, 15/01508-3, 15/25619-9)