Antônio José da Costa Filho

Antonio José da Costa Filho received a Bachelor degree in Physics from the University of São Paulo (USP) in 1994. After that he started his graduate program in the same university, concluding his Masters in 1996. His PhD project was developed both in São Carlos (Brazil), under the supervision of Prof. Otaciro Nascimento, and in Ithaca (USA), where he spent 3 years as a graduate student at Cornell University, working under Prof. Jack Freed´s supervision. In 2001 he received his PhD degree in Physics from the University of São Paulo and started working as an Assistant Professor at USP (Campus São Carlos). He is currently a Full Professor at USP-Ribeirão Preto and his research interests involve the investigation of interactions between biomolecules with emphasis on how the interaction between proteins and their ligands (substrates, inhibitors, and membranes) can lead to modulation/control of the protein function. More recently, he also got involved in projects seeking to identify how pharmacologically-relevant compounds (metal complexes and drugs) affect the organization of models for the cell membrane. To accomplish those objectives he makes use of a combined and interdisciplinary approach of experimental techniques such as magnetic resonance, circular dichroism, and microcalorimetry. In this context, Prof. Costa-Filho group has been pioneering the establishment of electron magnetic resonance methods in Brazil for the study of conformational changes in proteins, such as site-directed spin labelling and double electron-electron resonance (DEER). He has received several awards for his teaching skills as well as for contributions to his specific field of scientific interest. He is the current President of the Brazilian Biophysical Society (SBBf), vice-coordinator of the Institute for Advanced Studies (USP/Ribeirao Preto), and a former Affiliate Member of the Brazilian Academy of Sciences, and of theAcademy of Sciences for the Developing World (previous Third World Academy of Sciences ? TWAS). More information can be found at:

Área de Pesquisa:

Our group is mainly interested in applications of Electron Spin Resonance to biologically-relevant problems. Electron Spin Resonance (ESR) is a powerful technique that makes use of either transition metal ions or spin probes, usually involving stable nitroxide radicals bound to molecules such as phospholipids or cysteine residues in proteins, to monitor changes in the probe vicinity. Some advantages of spin-labeling ESR experiments are the possibility of employing a selective probe that has a simple ESR spectra and their high sensitivity to the molecular motion of the spin-bearing moiety. The changes in the nitroxide surroundings can be related to a variety of biologically-relevant processes such as protein conformational changes, lipid-protein interactions, and to the dynamic structure of biological and model membranes.

Electron Spin Resonance (ESR) has been recently experiencing a new era of great effervescence mainly due to the establishment of time-resolved methods (pulsed ESR) and to the use of modern DNA techniques to specifically spin-label macromolecules, which along with the more traditional continuous-wave (cw) EPR experiment, constitutes the so-called site-directed spin labeling (SDSL) methodology. Research in our group is related to projects combining ESR methods with interesting Biophysics problems. In general terms the problems we are interested in can be divided in three main areas:
(1) metal centers in enzyme structure;
(2) lipid-protein (and lipid-peptides) interactions;
(3) dynamic structure of lipid model membranes.