Perturbations on charged lipid bilayers induced by electric pulses, antimicrobial peptides and vesicles with opposite charge

• Grant number: 12/10442-8
• Support Opportunities: Regular Research Grants
• Start date: August 01, 2012
• End date: January 31, 2015
• Field of knowledge: Biological Sciences - Biophysics - Molecular Biophysics
• Principal Investigator: Karin Do Amaral Riske
• Grantee: Karin Do Amaral Riske
• Host Institution: Escola Paulista de Medicina (EPM). Universidade Federal de São Paulo (UNIFESP). Campus São Paulo. São Paulo , SP, Brazil

Abstract

Lipid bilayers have been extensively used as model systems of cellular membranes, with the purpose of studying in a controlled and independent way fundamental aspects of biological process involving membranes. The focus of this project is to study properties of negatively charged lipid bilayers when exposed to different perturbations: electric pulses, cationic vesicles and antimicrobial peptides. Sufficiently strong electric pulses cause the opening of transient pores in membranes. This phenomenon, known as electroporation, has been widely used in protocols of intracellular delivery of materials because it renders the plasma membrane transiently permeable. Another method of intracellular delivery commonly used is based on the fusion between synthetic liposomes and the plasma membrane. The opening of pores across the membrane or even its rupture can also be caused by antimicrobial peptides, which are part of the immune system of animals and plants and directly interact with the membrane of microorganisms because they usually exhibit a cationic and amphipathic character. The purposes of this project are to i) study the effects of electric pulses on anionic lipid bilayers, ii) evaluate the fusion efficiency between oppositely charged vesicles, mainly between small cationic and giant anionic vesicles, and iii) study the mechanism of action of antimicrobial peptides against charged model membranes. (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)

DOMINGUES, TATIANA M.; PEREZ, KATIA R.; MIRANDA, ANTONIO; RISKE, KARIN A.. Comparative study of the mechanism of action of the antimicrobial peptide gomesin and its linear analogue: The role of the beta-hairpin structure. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1848, n. 10, A, p. 2414-2421, OCT 2015. (08/57685-7, 12/10442-8)

CASADEI, BRUNA R.; DOMINGUES, CLEYTON C.; DE PAULA, ENEIDA; RISKE, KARIN A.. Direct Visualization of the Action of Triton X-100 on Giant Vesicles of Erythrocyte Membrane Lipids. BIOPHYSICAL JOURNAL, v. 106, n. 11, p. 2417-2425, JUN 3 2014. (10/18516-5, 12/10442-8)

LIRA, RAFAEL B.; DIMOVA, RUMIANA; RIEKE, KARIN A.. Giant Unilamellar Vesicles Formed by Hybrid Films of Agarose and Lipids Display Altered Mechanical Properties. BIOPHYSICAL JOURNAL, v. 107, n. 7, p. 1609-1619, OCT 7 2014. (12/10442-8, 13/07246-5)

LORENZON, E. N.; RISKE, K. A.; TROIANO, G. F.; DA HORA, G. C. A.; SOARES, T. A.; CILLI, E. M.. Effect of dimerization on the mechanism of action of aurein 1.2. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1858, n. 6, p. 1129-1138, JUN 2016. (12/15346-7, 12/10442-8)

DOMINGUES, TATIANA M.; PEREZ, KATIA R.; MIRANDA, ANTONIO; RISKE, KARIN A.. Comparative study of the mechanism of action of the antimicrobial peptide gomesin and its linear analogue: The role of the beta-hairpin structure. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1848, n. 10, p. 8-pg., 2015-10-01. (08/57685-7, 12/10442-8)