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Characterization of lipid dispersions of biological relevance: structures and interactions

Grant number: 17/25930-1
Support Opportunities:Regular Research Grants
Start date: April 01, 2018
End date: March 31, 2020
Field of knowledge:Physical Sciences and Mathematics - Physics - Condensed Matter Physics
Principal Investigator:Maria Teresa Moura Lamy
Grantee:Maria Teresa Moura Lamy
Host Institution: Instituto de Física (IF). Universidade de São Paulo (USP). São Paulo , SP, Brazil
Associated researchers:Evandro Luiz Duarte
Associated scholarship(s):19/08950-4 - Characterization of lipid dispersions of biological relevance: structures and interactions, BP.TT

Abstract

In the last many years, we have focused on the study of structural properties of amphiphilic dispersions, and its interactions with biomolecules. Accordingly, we built up a rather well-equipped laboratory, with the appropriate physical techniques. The present proposal is concerned about fundamental studies, but also focuses on the better understanding of the biological activity of the systems under study, the structure-activity relationship, aiming at the development of new drugs and/or vaccines. We propose the continuity of different subjects where we have significantly contributed, but where there are still many interesting open questions. The structural characterization of anionic lipid dispersions is one them, looking at the interactions present in the dispersions, inter and intra-aggregates. Another topic, is the spectroscopic properties of membrane fluorescent probes, like Laurdan and Prodan. In collaboration with biologists and biochemists, we aim the structural study of different vaccine adjuvants, and lipid-carriers of genetic material, in parallel with biological in vitro and in vivo assays. Still concomitant with biological assays, we propose the study of the interaction of a few biomolecules with model membranes, DNA and proteins. (AU)

Articles published in Agência FAPESP Newsletter about the research grant:
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VEICULO: TITULO (DATA)
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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)
MARQUEZIN, CASSIA A.; TERESA LAMY, M.; DE SOUZA, EDUARDO S.. Molecular collisions or resonance energy transfer in lipid vesicles? A methodology to tackle this question. JOURNAL OF MOLECULAR LIQUIDS, v. 341, . (21/01593-1, 18/20162-9, 14/50983-3, 17/25930-1)
VIGNOLI MUNIZ, GABRIEL S.; DE LA TORRE, I, LILIA; DUARTE, EVANDRO L.; LORENZON, ESTEBAN N.; CILLI, EDUARDO M.; BALAN, ANDREA; TERESA LAMY, M.. Interaction of synthetic antimicrobial peptides of the Hylin a1 family with models of eukaryotic structures: Zwitterionic membranes and DNA. BIOCHEMISTRY AND BIOPHYSICS REPORTS, v. 24, . (18/20162-9, 17/25930-1, 14/50983-3)
MATOS, FERNANDA LIMA; DUARTE, EVANDRO L.; MUNIZ, GABRIEL S. V.; MILAN-GARCES, ERIX ALEXANDER; COUTINHO, KALINE; LAMY, M. TERESA; DA CUNHA, ANTONIO R.. Spectroscopic characterization of different protonation/deprotonation states of Barbaloin in aqueous solution. SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY, v. 286, p. 11-pg., . (17/25930-1, 14/50983-3, 18/20162-9, 21/01593-1, 17/03910-9, 21/09016-3)
MUNIZ, GABRIEL S. VIGNOLI; SOUZA, MARIANA C.; DUARTE, EVANDRO L.; LAMY, M. TERESA. Comparing the interaction of the antibiotic levofloxacin with zwitterionic and anionic membranes: Calorimetry, fluorescence, and spin label studies. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1863, n. 7, p. 16-pg., . (18/20162-9, 17/25930-1, 14/50983-3)
MUNIZ, GABRIEL S. VIGNOLI; SOUZA, MARIANA C.; DUARTE, EVANDRO L.; LAMY, M. TERESA. omparing the interaction of the antibiotic levofloxacin with zwitterionic and anionic membranes: Calorimetry, fluorescence, and spin label studie. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1863, n. 7, . (18/20162-9, 17/25930-1, 14/50983-3)
MUNIZ, GABRIEL S. VIGNOLI; DUARTE, EVANDRO L.; LORENZON, ESTEBAN N.; CILLI, EDUARDO M.; LAMY, M. TERESA. What different physical techniques can disclose about disruptions on membrane structure caused by the antimicrobial peptide Hylin a1 and a more positively charged analogue. Chemistry and Physics of Lipids, v. 243, p. 16-pg., . (17/25930-1, 18/20162-9, 14/50983-3, 21/01593-1)