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RMBLab

Protein Biophysical Chemistry Group

Daniela C. Vaz

dvaz pic




PhD Researcher

Email: dvaz@ci.uc.pt

Daniela Vaz is currently a PhD researcher at the Center for Neuroscience and Cell Biology (CNC). Daniela started to work as a researcher still as an undergraduate student, under the supervision of prof. Mark Dickinson (Hull University, UK), where she conducted studies on yeast alcohol dehydrogenase. Then, she joined the CNC soon after completing her graduation in Biochemistry, in 1997. Since then, Daniela has collaborated in several research projects of the Structural and Computational Biology group, mainly through the study and characterization of proteins in solution. During her Master Degree in Cell Biology, she produced and expressed, in collaboration with Dr. Walter Sebald and Dr. Thomas Mueller, at the Biozentrum, (Wuerzburg University, Germany), several mutant proteins of interleukin-4 (IL-4), in order to characterize their functional, structural and thermodynamic properties. During her PhD in Biological Chemistry (at the University of Coimbra), she carried out work on the following subjects: i) unravelling the molecular mechanisms of protein aggregation and amyloid formation by the protein transthyretin (TTR); ii) determination of the tri-dimensional structure of various mutant proteins of interleukin-4 in solution, making use of multidimensional and triple resonance nuclear magnetic resonance (NMR) experiments, in collaboration with Dr. Christina Redfield, at the Oxford Centre for Molecular Sciences (OCMS), Oxford University (UK).

Presently, Vaz’s main research interests are:

  • protein structure and stability and its relationship to function and pathology;
  • biosensoring and molecular diagnosis in pathology;
  • application of biopolymers and biomaterials in tissue recovery and engineering.

Since 2008, Daniela Vaz is also a full time professor at the School of Health Sciences, in Leiria, Portugal, where she lectures Biochemistry, Biophysics and Biomaterials; integrates the Health Research Unit (UIS) and the Council of the Department of Biological Sciences, Mathematics, Informatics and Social Sciences, beyond coordinating scientific research projects also supervising the research work of undergraduate and master degree students.

Selected Publications
  • Jesus, C.S.H., Almeida, Z.L., Vaz, D.C., Faria, T.Q., Brito, R.M.M. (2016) "A New Folding Kinetic Mechanism for Human Transthyretin and the Influence of the Amyloidogenic V30M Mutation". Int. J. Mol. Sci. 17(9), 1428.

  • Pereira, R., Carvalho, A., Vaz, D.C., Gil, M.H., Mendes, A., Bártolo, P. (2013) "Development of novel alginate based hydrogel films for wound healing applications", International Journal of Biological Macromolecules, 52, pp. 221-230.

  • Jesus, C.S.H., Vaz, D.C., Saraiva, M.J.M. and Brito, R.M.M. (2012). "The V30M Amyloidogenic Mutation Decreases the Rate of Refolding Kinetics of the Tetrameric Protein Transthyretin", Spectroscopy: An International Journal 27 (5-6), pp. 343–348.

  • Pereira, R., Tojeira, A., Vaz, D.C., Mendes, A. and Bártolo, P. (2011) "Preparation anda Characterization of films based on alginate and Aloe vera", Int. J. Polym. Anal. Charact. 16(7), pp. 449-464. 

  • Vaz, D.C., Rodrigues, J.R., Sebald, W., Dobson, C.M., Brito, R.M.M. (2006) "Enthalpic and entropic contributions mediate the role of disulfide bonds on the conformational stability of interleukin-4", Protein Sci. 15(1), pp. 33-44. 

  • Quintas, A., Vaz, D.C., Cardoso, I., Saraiva, M.J., Brito, R.M.M. (2001) "Tetramer dissociation and monomer partial unfolding precedes protofibril formation in amyloidogenic transthyretin variants", J. Biol. Chem. 276(29), pp. 27207-27213.