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Proteins under fibrillation process: a structural and spectroscopic study of the influence of denaturating agents


In the present project it will be studied the structural and spectroscopic characteristics of proteins in solution during the fibrillation process. This project can be divided into two parts: a) one concerning the structural characterization of the fibril-like aggregates, and b) the second one regarding the study of the physical properties of the aggregates during the process of fiber formation, i.e., the study of the protein-protein interaction potential at such condition. It is important to mention that many neurodegenerative diseases are associated with the formation of amyloid-like fibrils and, so far, it is not clear yet what is (and how to model) the correct protein-protein interaction potential under these conditions. In order to obtain further information on these systems, we use two well-known model proteins: Lysozyme and Bovine Serum Albumin to characterize the protein-protein interaction potential during the process of fiber formation. It is important to mention that most of the proteins can form fibril-like structures, depending on the environmental condition that they are submitted. Nevertheless, the mechanism that governs the fibril-like structures formation is not kwon yet. In this context, the study of the protein-protein interaction potentials, from both theoretical and experimental point of view, can be a path to better understand this process. In order to get more information on this subject, we will use some spectroscopic techniques such as Zetta-Potential, Dynamic Light Scattering, Fluorescence in addition to small angle X-ray measurements. The induction of the formation of fibril-like aggregates will be made by different experimental conditions, such as changes in ionic strength (salt concentration), presence of external agents such as urea, surfactants and secondary structure-inducing agent, TFE. We hope to find out a characteristic behavior to the protein-protein interaction potential under these conditions. I believe that this project will give more information on the protofibril formation, in particular, on the attractive protein-protein interaction potential that leads to the aggregate formation. I would like to stress that I recently got a position in the Departamento de Física Geral, Instituto de Física - USP, where this project will be developed. (AU)

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Scientific publications (8)
(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)
SERAPHIM, V, THIAGO; NANO, NARDIN; CHEUNG, YIU WING SUNNY; ALUKSANASUWAN, SIRIPAT; COLLETI, CAROLINA; MAO, YU-QIAN; BHANDARI, VAIBHAV; YOUNG, GAVIN; HOLL, LARISSA; PHANSE, SADHNA; et al. ssembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexe. Structure, v. 30, n. 1, p. 156+, . (17/26131-5, 12/50161-8, 15/15822-1, 16/05019-0, 16/01603-9, 12/01953-9)
NANO, NARDIN; UGWU, FRANCISCA; SERAPHIM, V, THIAGO; LI, TANGZHI; AZER, GINA; ISAAC, METHVIN; PRAKESCH, MICHAEL; BARBOSA, LEANDRO R. S.; RAMOS, I, CARLOS H.; DATTI, ALESSANDRO; et al. Sorafenib as an Inhibitor of RUVBL2. BIOMOLECULES, v. 10, n. 4, . (16/05019-0, 15/15822-1, 12/50161-8, 12/01953-9)
MABANGLO, MARK F.; LEUNG, ELISA; VAHIDI, SIAVASH; SERAPHIM, V, THIAGO; EGER, BRYAN T.; BRYSON, STEVE; BHANDARI, VAIBHAV; ZHOU, JIN LIN; MAO, YU-QIAN; RIZZOLO, KAMRAN; et al. ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. COMMUNICATIONS BIOLOGY, v. 2, . (16/05019-0, 15/15822-1, 12/50161-8, 12/01953-9)
SERAPHIM, THIAGO V.; ALVES, MARINA M.; SILVA, INDJARA M.; GOMES, FRANCISCO E. R.; SILVA, KELLY P.; MURTA, SILVANE M. F.; BARBOSA, LEANDRO R. S.; BORGES, JULIO C.. Low Resolution Structural Studies Indicate that the Activator of Hsp90 ATPase 1 (Aha1) of Leishmania braziliensis Has an Elongated Shape Which Allows Its Interaction with Both N- and M-Domains of Hsp90. PLoS One, v. 8, n. 6, . (11/23110-0, 10/19242-6, 12/50161-8, 12/01953-9, 08/09025-8)
SILVA, NOELI S. M.; SERAPHIM, THIAGO V.; MINARI, KARINE; BARBOSA, LEANDRO R. S.; BORGES, JULIO C.. Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. International Journal of Biological Macromolecules, v. 108, p. 193-204, . (11/23110-0, 12/50161-8, 17/07335-9, 12/01953-9, 15/15822-1, 14/07206-6, 13/25646-0)
WONG, KEITH S.; MABANGLO, MARK F.; SERAPHIM, THIAGO V.; MOLLICA, ANTONIO; MAO, YU-QIAN; RIZZOLO, KAMRAN; LEUNG, ELISA; MOUTAOUFIK, MOHAMED T.; HOELL, LARISSA; PHANSE, SADHNA; et al. Acyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death. Cell Chemical Biology, v. 25, n. 8, p. 1017+, . (16/05019-0, 12/01953-9, 15/15822-1)
QUEL, NATALIA G.; PINHEIRO, GLAUCIA M. S.; RODRIGUES, LUIZ FERNANDO DE C.; BARBOSA, LEANDRO R. S.; HOURY, WALID A.; RAMOS, I, CARLOS H.. Heat shock protein 90 kDa (Hsp90) from Aedes aegypti has an open conformation and is expressed under heat stress. International Journal of Biological Macromolecules, v. 156, p. 522-530, . (17/26131-5, 16/05019-0, 15/15822-1, 14/25967-4, 12/01953-9)
QUEL, NATALIA G.; RODRIGUES, LUIZ FERNANDO DE C.; ARAGAO, ANNELIZE Z. B.; PINHEIRO, GLAUCIA M. S.; CAMACHO, RAFAEL P.; SOUTO, DENIO E. P.; KUBOTA, LAURO T.; BARBOSA, LEANDRO R. S.; RAMOS, CARLOS H. I.. Insights into the structure and function of the C-terminus of SGTs (small glutamine-rich TPR-containing proteins): A study of the Aedes aegypti homolog. Biochimie, v. 187, p. 131-143, . (16/05019-0, 12/01953-9, 14/25967-4, 17/26131-5, 15/15822-1)

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