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Probing the nanobiointerface: dynamic, structure and binding ratio of plasma proteins adsorbed onto polymeric micelles and polymersomes

Grant number: 17/19079-7
Support Opportunities:Scholarships in Brazil - Master
Effective date (Start): March 01, 2018
Effective date (End): February 29, 2020
Field of knowledge:Physical Sciences and Mathematics - Chemistry - Physical-Chemistry
Acordo de Cooperação: Coordination of Improvement of Higher Education Personnel (CAPES)
Principal Investigator:Fernando Carlos Giacomelli
Grantee:Fernando Augusto de Oliveira
Host Institution: Centro de Ciências Naturais e Humanas (CCNH). Universidade Federal do ABC (UFABC). Ministério da Educação (Brasil). Santo André , SP, Brazil
Associated scholarship(s):18/21272-2 - Exploiting the relevance of the protein corona on the cellular uptake of polymeric micelles and polymersomes, BE.EP.MS


The investigations will be devoted to the influence of polymeric nanoparticles' morphology on the interaction and adsorption with plasma proteins. Initially, polymeric micelles and polymersomes will be produced from synthesized pH-responsive or biodegradable block copolymers made as PHPMAm-b-PDPAn, PEOm-b-PLAn and PAAm-b-PSn. The assemblies will be deeply characterized by using a variety of scattering techniques (dynamic light scattering - DLS, static light scattering - SLS, electrophoretic light scattering - ELS and small-angle x-ray scattering - SAXS) besides transmission electron microscopy (TEM). Subsequently, it will be evaluated the adsorption of different plasma proteins onto the surface of the produced polymeric assemblies with further discussions in relation with structural features, particularly their morphology. The interaction and adsorption of distinct plasma proteins (HSA, IgG, fibrinogen, APoA1 and lysozyme) onto polymeric micelles and vesicles will be investigated taking into account the binding dynamics, binding affinity, binding ratio as well as protein conformational changes due to binding. The binding dynamics will be monitored essentially via dynamic and electrophoretic light scattering measurements. Accordingly, changes in size, size distribution and surface charge will be monitored as a function of time. The static light scattering measurements will be employed to determine the molecular weight of the nanoparticle-protein complexes and consequently the binding ratio. Thermodynamic informations such as number of binding sites and binding constants will be determined via isothermal titration calorimetry (ITC) and therefore it will possibly allow us to get informations related to the mechanisms of binding and primary intermolecular forces involved. Finally, possible protein conformational changes due to the adsorption phenomena will be probed by circular dichroism, fluorescence and Raman spectroscopy. (AU)

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Scientific publications
(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)
DE OLIVEIRA, FERNANDO A.; ALBUQUERQUE, LINDOMAR J. C.; RISKE, KARIN A.; JAGER, ELIEZER; GIACOMELLI, FERNANDO C.. Outstanding protein-repellent feature of soft nanoparticles based on poly(N-(2-hydroxypropyl) methacrylamide) outer shells. Journal of Colloid and Interface Science, v. 574, p. 260-271, . (17/19079-7, 18/21272-2, 17/00459-4)

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