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Biophysical studies of the structure/function of antimicrobial peptides and enzymes isolated from extremophile organisms

Grant number: 15/50347-2
Support type:Regular Research Grants
Duration: October 01, 2015 - March 31, 2018
Field of knowledge:Biological Sciences - Biophysics - Molecular Biophysics
Cooperation agreement: BBSRC, UKRI - FAPPA
Principal Investigator:Ana Paula Ulian de Araujo
Grantee:Ana Paula Ulian de Araujo
Principal investigator abroad: Bonnie Ann Wallace
Institution abroad: University of London, England
Home Institution: Instituto de Física de São Carlos (IFSC). Universidade de São Paulo (USP). São Carlos , SP, Brazil

Abstract

This project would use novel developments for spectroscopic characterization of these AMP in liposomes, lipid films and lipid monolayers to establish the mechanism of action and optimize the design of novel related peptides as bacteriocins. The project will also focus on the identification and characterisation of new hyper-stable enzymes isolated from petrochemical sources. Extremophiles isolated from hot oilfield waters produce a range pf enzymes that exhibit both thermostability and stability in non- aqueous solvents, that give them potential for use in industrial applications where their unique properties are compatible with bioprocessing and biomodification requirements. This project will examine the thermal stability and environmental stability factors associated with enzymes from extremophile isolates using a range of novel spectroscopic methods, including SRCD and fluorescence. The functional enzymatic properties would be correlated with structural features, in particular in organic, lipophilic and other non-aqueous milleux. (AU)

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)
FELIZATTI, ANA P.; ZERAIK, ANA E.; BASSO, LUIS G. M.; KUMAGAI, PATRICIA S.; LOPES, JOSE L. S.; WALLACE, B. A.; ARAUJO, ANA P. U.; DEMARCO, RICARDO. Interactions of amphipathic alpha-helical MEG proteins from Schistosoma mansoni with membranes. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, v. 1862, n. 3 MAR 1 2020. Web of Science Citations: 0.
KUMAGAI, PATRICIA S.; SOUSA, VICTOR K.; DONATO, MARESSA; ITRI, ROSANGELA; BELTRAMINI, LEILA M.; ARAUJO, ANA P. U.; BUERCK, JOCHEN; WALLACE, B. A.; LOPES, JOSE L. S. Unveiling the binding and orientation of the antimicrobial peptide Plantaricin 149 in zwitterionic and negatively charged membranes. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, v. 48, n. 7, p. 621-633, OCT 2019. Web of Science Citations: 1.
KUMAGAI, PATRICIA S.; GUTIERREZ, RAISSA F.; LOPES, JOSE L. S.; MARTINS, JULIA M.; JAMESON, DAVID; CASTRO, ALINE M.; MARTINS, LUIZ F.; DEMARCO, RICARDO; BOSSOLAN, NELMA R. S.; WALLACE, B. A.; ARAUJO, ANA P. U. Characterization of esterase activity from an Acetomicrobium hydrogeniformans enzyme with high structural stability in extreme conditions. EXTREMOPHILES, v. 22, n. 5, p. 781-793, SEP 2018. Web of Science Citations: 3.
KUMAGAI, PATRICIA S.; DEMARCO, RICARDO; LOPES, JOSE L. S. Advantages of synchrotron radiation circular dichroism spectroscopy to study intrinsically disordered proteins. EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, v. 46, n. 7, SI, p. 599-606, OCT 2017. Web of Science Citations: 11.
LOPES, JOSE L. S.; YONEDA, JULIANA S.; MARTINS, JULIA M.; DEMARCO, RICARDO; JAMESON, DAVID M.; CASTRO, ALINE M.; BOSSOLAN, NELMA R. S.; WALLACE, B. A.; ARAUJO, ANA P. U. Environmental Factors Modulating the Stability and Enzymatic Activity of the Petrotoga mobilis Esterase (PmEst). PLoS One, v. 11, n. 6 JUN 28 2016. Web of Science Citations: 4.
DA HORA, G. C. A.; ARCHILHA, N. L.; LOPES, J. L. S.; MUELLER, D. M.; COUTINHO, K.; ITRI, R.; SOARES, T. A. Membrane negative curvature induced by a hybrid peptide from pediocin PA-1 and plantaricin 149 as revealed by atomistic molecular dynamics simulations. SOFT MATTER, v. 12, n. 43, p. 8884-8898, 2016. Web of Science Citations: 3.

Please report errors in scientific publications list by writing to: cdi@fapesp.br.