Sebastián Tanco
  • Medical Biotechnology Center, VIB, Belgium
Research focus
  • Plant science
Personal information


Ph.D. in Protein Structure and Function, Institut de Biotecnologia i de Biomedicina, Universitat Autonoma de Barcelona, 2012

Current Position

Postdoctoral researcher at the Medical Biotechnology Center – VIB and at the Department of Biochemistry, Ghent University, Ghent, Belgium


  1. Lufrano, D., Cotabarren, J., Garcia-Pardo, J., Fernandez-Alvarez, R., Tort, O., Tanco, S., Aviles, F. X., Lorenzo, J. and Obregon, W. D. (2015). Biochemical characterization of a novel carboxypeptidase inhibitor from a variety of Andean potatoes. Phytochemistry 120: 36-45.
  2. Fait, M. E., Garrote, G. L., Clapes, P., Tanco, S., Lorenzo, J. and Morcelle, S. R. (2015). Biocatalytic synthesis, antimicrobial properties and toxicity studies of arginine derivative surfactants. Amino Acids 47(7): 1465-1477.
  3. Tanco, S., Gevaert, K. and Van Damme, P. (2015). C-terminomics: Targeted analysis of natural and posttranslationally modified protein and peptide C-termini. Proteomics 15(5-6): 903-914.
  4. Tanco, S., Tort, O., Demol, H., Aviles, F. X., Gevaert, K., Van Damme, P. and Lorenzo, J. (2015). C-terminomics screen for natural substrates of cytosolic carboxypeptidase 1 reveals processing of acidic protein C termini. Mol Cell Proteomics 14(1): 177-190.
  5. Tort, O., Tanco, S., Rocha, C., Bieche, I., Seixas, C., Bosc, C., Andrieux, A., Moutin, M. J., Aviles, F. X., Lorenzo, J. and Janke, C. (2014). The cytosolic carboxypeptidases CCP2 and CCP3 catalyze posttranslational removal of acidic amino acids. Mol Biol Cell 25(19): 3017-3027.
  6. Tanco, S., Lorenzo, J., Garcia-Pardo, J., Degroeve, S., Martens, L., Aviles, F. X., Gevaert, K. and Van Damme, P. (2013). Proteome-derived peptide libraries to study the substrate specificity profiles of carboxypeptidases. Mol Cell Proteomics 12(8): 2096-2110.
  7. Otero, A., Rodriguez de la Vega, M., Tanco, S., Lorenzo, J., Aviles, F. X. and Reverter, D. (2012). The novel structure of a cytosolic M14 metallocarboxypeptidase (CCP) from Pseudomonas aeruginosa: a model for mammalian CCPs. FASEB J 26(9): 3754-3764.
  8. Benitez, J., Becco, L., Correia, I., Leal, S. M., Guiset, H., Pessoa, J. C., Lorenzo, J., Tanco, S., Escobar, P., Moreno, V., Garat, B. and Gambino, D. (2011). Vanadium polypyridyl compounds as potential antiparasitic and antitumoral agents: new achievements. J Inorg Biochem 105(2): 303-312.
  9. Tanco, S., Zhang, X., Morano, C., Aviles, F. X., Lorenzo, J. and Fricker, L. D. (2010). Characterization of the substrate specificity of human carboxypeptidase A4 and implications for a role in extracellular peptide processing. J Biol Chem 285(24): 18385-18396.
  10. Tanco, S., Arolas, J. L., Guevara, T., Lorenzo, J., Aviles, F. X. and Gomis-Ruth, F. X. (2010). Structure-function analysis of the short splicing variant carboxypeptidase encoded by Drosophila melanogaster silver. J Mol Biol 401(3): 465-477.
  11. Rodriguez de la Vega, M., Sevilla, R. G., Hermoso, A., Lorenzo, J., Tanco, S., Diez, A., Fricker, L. D., Bautista, J. M. and Aviles, F. X. (2007). Nna1-like proteins are active metallocarboxypeptidases of a new and diverse M14 subfamily. FASEB J 21(3): 851-865.
  12. Benitez, G., Vericat, C., Tanco, S., Remes Lenicov, F., Castez, M. F., Vela, M. E. and Salvarezza, R. C. (2004). Role of surface heterogeneity and molecular interactions in the charge-transfer process through self-assembled thiolate monolayers on Au(111). Langmuir 20(12): 5030-5037.
  13. Vericat, C., Remes Lenicov, F., Tanco, S., Andreasen, G., Vázquez, L., Vela, M. E. and Salvarezza, RC (2003). Binary self-assembled of alkanethiols on Au(111) studied by STM. Acta Microscopica 12: 78-82.
  14. Vericat, C., Remes Lenicov, F., Tanco, S., Andreasen, G.., Vela, M. E. and Salvarezza, R. C. (2002). Building complex twodimensional structures: methylene blue on self-assembled monolayer-covered Au(111). Journal of Physical Chemistry B 106: 9114-9121.
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