Understanding the molecular interactions between ionic liquids and biopharmaceuticals: the key for a proper design of downstream processing

• Grant number: 18/50009-8
• Support type: Regular Research Grants
• Duration: June 01, 2018 - May 31, 2020
• Field of knowledge: Engineering - Chemical Engineering - Chemical Process Industries
• Cooperation agreement: Australian Technology Network of Universities (ATN)
• Mobility Program: SPRINT - Projetos de pesquisa - Mobilidade
• Principal researcher: Jorge Pereira
• Grantee: Jorge Pereira
• Principal researcher abroad: Tamar Graves
• Institution abroad: RMIT University, Melbourne, Australia
• Home Institution: Faculdade de Ciências Farmacêuticas (FCFAR). Universidade Estadual Paulista (UNESP). Campus de Araraquara. Araraquara , SP, Brazil
• Associated research grant: 14/16424-7 - Optimization and scale-up of liquid-liquid extraction process with ionic liquids (ILs) as a sustainable tool for the separation of the anti-leukemia biopharmaceutical L-asparaginase (ASPase), AP.JP

Abstract

Pharmaceutical industry have been developing more sustainable, biocompatible and efficient biopharmaceuticals separation and purification technologies. Thus, and in a context where sustainable processes and ecological transition is promoted in many developed countries, Aqueous Two-Phase Systems (ATPS) composed of Ionic Liquids (ILs) have appeared in the past years to be a breakthrough technique for the bioproduct separation and extraction from complex media. Many data are available for the extraction of bioproducts using IL-based ATPS. Nevertheless, there is hardly any understanding of the extraction and separation mechanisms governing the solutes partitioning using these systems, particularly, due to the complex IL-protein interactions. Solvent-protein interactions are extremely important to control, maintain or enhance the protein stability and activity, and thus, a proper choice of the IL used as solvent is the key for designing suitable separation or biocatalytic processes. The main goals of the present joint proposal are to 1) characterize, reveal and understand the main interactions that occur at a molecular level in aqueous solutions of ILs and proteins, and 2) use this knowledge to develop stable IL- based platforms for the recovery of biopharmaceuticals. (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)

DOS SANTOS, NATHALIA VIEIRA; SAPONI, CAROLINA FALASCHI; RYAN, TIMOTHY M.; PRIMO, FERNANDO L.; GREAVES, TAMAR L.; PEREIRA, JORGE F. B. Reversible and irreversible fluorescence activity of the Enhanced Green Fluorescent Protein in pH: Insights for the development of pH-biosensors. International Journal of Biological Macromolecules, v. 164, p. 3474-3484, DEC 1 2020. Web of Science Citations: 0.

FARIAS, FABIANE OLIVEIRA; PEREIRA, JORGE F. B.; COUTINHO, JOAO A. P.; IGARASHI-MAFRA, LUCIANA; MAFRA, MARCOS R. Understanding the role of the hydrogen bond donor of the deep eutectic solvents in the formation of the aqueous biphasic systems. Fluid Phase Equilibria, v. 503, JAN 1 2020. Web of Science Citations: 1.

MAGRI, AGNES; PECORARI, THAINA; PEREIRA, MATHEUS M.; CILLI, EDUARDO M.; GREAVES, TAMAR L.; PEREIRA, JORGE F. B. Enhancing the Biocatalytic Activity of L-Asparaginase Using Aqueous Solutions of Cholinium-Based Ionic Liquids. ACS SUSTAINABLE CHEMISTRY & ENGINEERING, v. 7, n. 24, p. 19720-19731, DEC 16 2019. Web of Science Citations: 0.

DOS SANTOS, NATHALIA VIEIRA; SAPONI, CAROLINA FALASCHI; GREAVES, TAMAR LOUISE; BRANDAO PEREIRA, JORGE FERNANDO. Revealing a new fluorescence peak of the enhanced green fluorescent protein using three-dimensional fluorescence spectroscopy. RSC ADVANCES, v. 9, n. 40, p. 22853-22858, AUG 1 2019. Web of Science Citations: 0.

LOPES, CAMILA; DOS SANTOS, NATHALIA VIEIRA; DUPONT, JANA; PEDROLLI, DANIELLE BISCARO; VALENTINI, SANDRO ROBERTO; SANTOS-EBINUMA, VALERIA DE CARVALHO; BRANDAO PEREIRA, JORGE FERNANDO. Improving the cost effectiveness of enhanced green fluorescent protein production using recombinant Escherichia coli BL21 (DE3): Decreasing the expression inducer concentration. Biotechnology and Applied Biochemistry, v. 66, n. 4, p. 527-536, JUL 2019. Web of Science Citations: 0.