Pedro M. Nieto Mesa
Group: Glycosystem Laboratory
Position: CSIC Research Professor
Contact
Tel. ext: 446268
Laboratory: L S002
Office: D S011
Email:
ORCID: 0000-0002-4074-9011
Biography
Pedro M. Nieto obtained his PhD in the Universidad Autónoma de Madrid in 1994 under the supervisión of Prof. Javier de Mendoza and Dr Pilar Prados in Supramolecular Chemistry of calix[6]arenes with honours. After he did postdoctoral work in the National Institute for Medical Research from the Medical Research Council with Dr Jim Feeney in the Department of Molecular Structure, working in Protein NMR, I was interested in the dynamic aspects and in the relationship between structure and dynamics. In 1997, I moved to the Instituto de Investigaciones Químicas in Sevilla, joining the “Grupo de Carbohidratos” with Prof. Manuel Martín-Lomas, where I became responsible for the structural projects. In 2001, I was awarded a Ramón y Cajal Fellowship and became a CSIC tenured Scientist in 2002. Since then, I have been working in different aspects of the Molecular Recognition of Biomolecules, always from a structural perspective and combining experimental NMR data with theoretical calculations.
During this time, I have been awarded six Plan Nacional, two Junta de Andalucia, and two research contracts as PI, among other participations as a member of the research team. In addition, I have been taking on duties as the person responsible for the NMR facilities of the IIQ. In 2010, I was promoted to CSIC Researcher. From 2012 until 2020, I was Scientific Director of the Biointeractomic Platform of cicCartuja, participating in funding requests, infrastruture definition, and setup, ceasing in 2020.
Research interests
1. Molecular basis of the molecular recognition of carbohydrates by proteins using NMR and Computational Tools (MD, MD-tar and Docking) in systems in fast exchange.
1.1. Glycosaminoglycans and Growth Factors (FGF-1 &2, ECP, MDK, PTN)
1.2. Interactions between GAG, and mimetics thereoff and C-Lectins (DC-SIGN and Langerin)
2. New NMR sequences and tools for structural elucidation.
3. NMR methodological aspects on redox proteins.
Selected publications
- Angulo, J., and P. M. Nieto. “STD-NMR: Application to Transient Interactions between Biomolecules-a Quantitative Approach.” European Biophysics Journal 40, no. 12 (2011): 1357–69. https://doi.org/10.1007/s00249-011-0749-5.
- Angulo, J., R. Ojeda, J. L. de Paz, et al. “The Activation of Fibroblast Growth Factors (FGFs) by Glycosaminoglycans: Influence of the Sulfation Pattern on the Biological Activity of FGF-1.” ChemBioChem 5, no. 1 (2004): 55–61. https://doi.org/10.1002/cbic.200300696.
- Canales, A., J. Angulo, R. Ojeda, et al. “Conformational Flexibility of a Synthetic Glycosylaminoglycan Bound to a Fibroblast Growth Factor. FGF-1 Recognizes Both the (1)C(4) and (2)S(O) Conformations of a Bioactive Heparin-like Hexasaccharide.” Journal of the American Chemical Society 127, no. 16 (2005): 5778–79. https://doi.org/10.1021/ja043363y.
- Diaz-Moreno, I., P. M. Nieto, R. Del Conte, et al. “A Non-Damaging Method to Analyze the Configuration and Dynamics of Nitrotyrosines in Proteins.” Chemistry – A European Journal 18, no. 13 (2012): 3872–78. https://doi.org/10.1002/chem.201103413.
- García-Jiménez, M. José, Sergi Gil, Pedro Domínguez-Rodriguez, et al. “Interaction Studies by NMR on the Multivalent Interaction between Chondroitin Sulfate E Derivatives and the Langerin Receptor.” Organic & Biomolecular Chemistry 23, no. 38 (2025): 8704–18. https://doi.org/10.1039/D5OB00845J.
- Nieto, P. M., B. Birdsall, W. D. Morgan, T. A. Frenkiel, A. R. Gargaro, and J. Feeney. “Correlated Bond Rotations in Interactions of Arginine Residues with Ligand Carboxylate Groups in Protein Ligand Complexes.” FEBS Letters 405, no. 1 (1997): 16–20. https://doi.org/10.1016/S0014-5793(97)00147-6.
- Perez, Serge, Olga Makshakova, Jesus Angulo, et al. “Glycosaminoglycans: What Remains To Be Deciphered?” JACS Au 3, no. 3 (2023): 628–56. https://doi.org/10.1021/jacsau.2c00569.
- Porkolab, V., E. Chabrol, N. Varga, et al. “Rational-Differential Design of Highly Specific Glycomimetic Ligands: Targeting DC-SIGN and Excluding Langerin Recognition.” ACS Chemical Biology 13, no. 3 (2018): 600–608. https://doi.org/10.1021/acschembio.7b00958.
- Solera, C., G. Macchione, S. Maza, et al. “Chondroitin Sulfate Tetrasaccharides: Synthesis, Three-Dimensional Structure and Interaction with Midkine.” Chemistry – A European Journal 22, no. 7 (2016): 2356–69. https://doi.org/10.1002/chem.201504440.

