Dr. Ana María Fernández Escamilla

Department: Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche (IDiBE) / Protein Architecture Group

Phone: +34 965 222 088

Email: ana.fernandez@umh.es

Current Position: Associate  Professor, Biochemistry and Molecular Biology Department, Universidad Miguel Hernández.

Research Fields

  • Protein engineering.

  • Protein-ligand binding interactions and protein-protein interaction.

  • Molecular modeling.

  • Biochemical, biophysical and structural characterization of proteins.

  • New amyloids: exploitation in biomedicine, food security (food allergy) and sustainable agriculture.

  • Bacterial biosensor development for detection of toxic and antimicrobial compounds.

  • Characterization of the molecular mechanisms involved in microorganism-environment interaction.

Representative Publications

  • Fernandez, A. M., Villegas, V, Martínez, J. C., van Nuland, N. A. J, Conejero-Lara, F., Avilés, F. X., Serrano, L., Filimonov, V. V. & Mateo, P. L. Thermodynamic analysis of helix- engineered forms of the activation domain of human procarboxypeptidase A2. European Journal of Biochemistry. (2000), 267, 5891-5899.

  • Fernandez-Escamilla A. M., Cheung, M. S., Vega, M. C., Wilmanns, M., Onuchic, J. N., Serrano, L. Solvation in protein folding analysis, combination of theoretical and experimental approaches. Proceedings of the National Academy of Science of the United States of America: PNAS (2004), 101, 2834-2839.

  • Fernandez-Escamilla A. M., Rosseau, F., Schymkowitz, J. & Serrano, L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins. Nature Biotechnology (2004), 22, 1302-1306.

  • Fernandez-Escamilla A.M., Ventura S., Serrano L. & Jiménez M.A. Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains. Protein Science (2006), 15, 2278-2289.

  • Fernandez-Escamilla AM.*, Sánchez-Hidalgo M.*, Martínez-Bueno M., Valdivia E., Serrano L. & Maqueda M. Conformational stability and activity of circular enterocin AS-48 derivatives. Protein and Peptide Letters 2010; 17(6):708-14.


Patents and Available Technologies

  • TANGO. A computer algorithm designed to predict aggregation-nucleating regions in proteins as well, the effect of mutations and environmental conditions on the aggregation propensity of these regions. We derived a statistical mechanics algorithm, TANGO, based on simple physico-chemical principles of secondary structure formation extended by the assumption that the core regions of an aggregate are fully buried. TANGO was benchmarked against 175 peptides of over 20 proteins and was able to predict the sequences experimentally observed to contribute to the aggregation of these proteins. Further TANGO correctly predicts the aggregation propensities of several disease-related mutations in the Alzheimer’s b-peptide. Our algorithm, therefore, opens the possibility to screen large databases for potentially disease-related aggregation motifs as well as to optimize recombinant protein yields by rationally out-designing protein aggregation.

Company Agreements

  • Detection of toxic compounds by the bacterial biosensor based on the TtgR repressor of Pseudomonas putida DOT -T1E. Financial Entities: GRONTAL Biotechnological Solutions S.L. and Spanish National Research Council (CSIC). Principal Investigator: Ana María Fernández Escamilla.

Instituto de Investigación, Desarrollo e Innovación en Biotecnología Sanitaria de Elche

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Av/ de la Universidad, s/n

03202 Elche, Alicante



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