Jesús Angulo Álvarez

Group: Biomolecular interactions and structural glycobiology

Position: CSIC Scientifical Researcher

Contact

Tel. ext: 446266

Laboratory: L E110

Office: D 220

Email:

ORCID: 0000-0001-7250-5639

🌐 Angulo Lab

Biography

Jesús Angulo is a Investigador Científico-CSIC at the Institute for Chemical Research (IIQ, CSIC/University of Seville) since December 2021. Previously, he was Beatriz Galindo Senior Distinguished Researcher in the Department of Organic Chemistry at the University of Seville (December 2019 – December 2021) and Associate Professor at the University of East Anglia (UEA), Norwich, United Kingdom, where he started his research group in 2013. During his training, he obtained a pre-doctoral fellowship from the Ramón Areces Foundation at the IIQ (1999-2002), a Marie Curie Intra-European Individual postdoctoral fellowship at the University of Lübeck, Germany (2003-2005), a Juan de la Cierva postdoctoral fellowship at the CSIC (2006-2008), and a Ramón y Cajal contract (2008-2013) at the CSIC. His scientific career began at the CSIC (Seville) in the laboratory of Prof. M. Martín-Lomas, where he completed his doctoral thesis (2002) under the supervision of Dr. Pedro M. Nieto, focused on carbohydrate chemistry and the structural glycobiology of glycosaminoglycans (GAGs). In Lübeck (2003), he specialized in transfer NMR for protein–ligand interactions with Prof. Thomas Peters.

In 2006, he returned to the CSIC (Seville) with a Marie Curie reintegration grant to work on interactions of GAGs, glycomimetics, and glyconanoparticles with immunological receptors. From August 2013 to December 2019, his group at the UEA developed new NMR and computational methods for studying interactions, applied to systems such as the gut microbiota, pathogen infection (Salmonella), carbohydrate hydrolases, and new applications of STD NMR to hydrogels. Since December 2019, his group at the IIQ has focused on generating new spectroscopic approaches combined with computational chemistry to obtain 3D structures of weak ligand–protein complexes, aimed at the study of protein–glycan interactions and fragment-based drug discovery (FBDD). His contributions include: (i) Jesús was a pioneer in determining protein–ligand affinities by STD NMR, a methodology that has been widely adopted; (ii) he was the first to demonstrate the use of STD NMR to characterize multimodal ligand binding; (iii) he developed the DEEP-STD NMR methodology to determine the bioactive orientation of the ligand in the active site; (iv) he developed the RedMat software for 3D model validation; (v) he demonstrated the applicability of RedMat for interaction studies in membrane proteins in living cells; and (vi) he developed the “EPM-STD NMR (Epitope Perturbation by Mutation STD NMR)” methodology for determining the structures of weak complexes.

He received the “Best PhD Supervisor 2019” award from the University (UEA), Norwich. He is currently an Honorary Professor at the UEA, has been a Visiting Professor at the Università degli Studi di Milano, is Scientific Director of the Biomolecular Interactions Platform (CSIC), and President of the Specialized NMR Group (GERMN) of the RSEQ.

Research interests

• Structural characterization of Ligand Receptor interactions by NMR Spectroscopy

          – Weak protein-ligand interactions. Fragment based drug discovery.

          – Carbohydrate-Protein interactions. Carbohydrates in drug-delivery.

          – Drug-carrier interactions.

          – Ligand-based NMR for “in-cell” ligand-protein interactions

• Structure and dynamics of biologically active small/medium-sized molecules

Selected publications

• Nepravishta., et al. “Fast and reliable NMR-based fragment scoring for drug discovery “. Journal of the American Chemical Society. 2025, , 147, 44, 40296–40304.
• Monaco., et al. “On-Cell Saturation Transfer Difference NMR Spectroscopy on Ion Channels: Characterizing Negative Allosteric Modulator Binding Interactions of P2X7”. Journal of the American Chemical Society. 2025, 147, 32400−32411
• Nepravishta., et al. “Fast Quantitative Validation of 3D Models of Low-Affinity Protein-Ligand Complexes by STD NMR Spectroscopy”. Journal of Medicinal Chemistry, 2024, 67, 10025−10034.
• Silva-Díaz A., et al. “Fluorinated Man(9) as a High Mannose Mimetic to Unravel Its Recognition by DC-SIGN Using NMR “. Journal of the American Chemical Society. 2023, 145, 26009.
• Monaco S., et al. “Imaging Saturation Transfer Difference (STD) NMR: Affinity and Specificity of Protein-Ligand Interactions from a Single NMR Sample”. Journal of the American Chemical Society. 2023, 145, 16391.
• Bell, A., et al. “Elucidation of a novel sialic acid metabolism pathway in mucus-foraging bacteria unravels mechanisms of adaptation to the gut”. Nature Microbiology. 2019, 4, 2393
• Park, J., et al. “Structural basis for arginine glycosylation of host substrates by bacterial effector proteins”. Nature Communications. 2018, 9, 4283.
• Monaco, S., Tailford, L. E., Juge, N. & Angulo, J. “Differential Epitope Mapping by STD NMR Spectroscopy to Reveal the Nature of Protein–Ligand Contacts”. Angewandte Chemie International Edition 2017, 56, 48, pp. 15289.
• Owen, C. D., et al. “Unravelling the specificity and mechanism of sialic acid recognition by the gut symbiont Ruminococcus gnavus”. Nature Communications. 2017, 8, 2196.
• Muñoz-García, J. C., et al. “Langerin-Heparin Interaction: Two BindingSites for Small and Large Ligands by a combination of NMR Spectroscopy and Cross-Linking Mapping Experiments”. Journal of the American Chemical Society. 2015, 137, 4100.