October 2026 Webinar on Protein and Peptide Science

Prof Javier Montenegro, University of Santiago de Compostela 

Title: Supramolecular Dynamic Chemistry for membrane transport and Biomimetic Systems 

Our research group is interested in the application of supramolecular chemistry to understand and manipulate biology. [1,2] Our work philosophy is based in the importance of weak and non-covalent forces to control the shape and the topology of biomolecules, which are governed by the principles described by supramolecular chemistry. These supramolecular lessons can then be applied to control the properties and function of biomolecules. We believe that by modulating the shape we can mimic, control and improve functional behaviour. With focus in supramolecular interactions for artificial membranes and tubular composites, we investigate the construction of synthetic systems for controlling and emulating biology and life-like soft systems. [3-8] 

[1] Fuertes, A.; Juanes, M.; Granja, J.R.; Montenegro, J. Chem. Commun. 2017, 53, 7861–7871. 

[2] Lostalé-Seijo, I.; Montenegro, J. Nat. Rev. Chem. 2018, 2, 258–277. b) Pérez-Pérez, M.; Fuertes, A.; Montenegro, J. Curr. Opin. Chem. Biol. 2025, 78, 102497. 

[3] Gallego, I.; Ramos-Soriano, J.; Méndez-Ardoy, A.; Cabrera-González, J.; Lostalé-Seijo, I.; Illescas, B.M.; Reina, J.J.; Martín, N.; Montenegro, J. Angew. Chem. Int. Ed. 2022, 61, e202210043. 

[4] Fernández-Caro, H.; Méndez-Ardoy, A.; Montenegro, J. Nanoscale 2022, 14, 3599–3608. 

[5] Insua, I.; Bergueiro, J.; Méndez-Ardoy, A.; Lostalé-Seijo, I.; Montenegro, J. Chem. Sci. 2022, 13, 3057–3068. b) Insua, I.; Cardellini, A.; Díaz, S.; Bergueiro, J.; Capelli, R.; Pavan, G.M.; Montenegro, J. Chem. Sci. 2023, 14, 14074–14081. 

[6] Bayón-Fernández, A.; Méndez-Ardoy, A.; Álvarez-Lorenzo, C.; Granja, J.; Montenegro, J. J. Mater. Chem. B 2023, 11, 606–617. b) Folgar-Cameán, Y.; Torralba-Maldonado, D.; Fulias-Guzmán, P.; Pazo, M.; Máximo-Moreno, I.; Royo, M.; Illa, O.; Montenegro, J. J. Mater. Chem. B 2025, 13, 3365–3373. c) García Coll, J.; Ali, L.M.A.; Montenegro, J.; Bettache, N.; Ulrich, S. Chem. Commun. 2025, 61, 4050–4053. 

[7] Barba-Bon, A.; Salluce, G.; Lostalé-Seijo, I.; Assaf, K.I.; Hennig, A.; Montenegro, J.; Nau, W.M. Nature 2022, 603, 637–642. b) Chen, Y.; Barba-Bon, A.; Grüner, B.; Winterhalter, M.; Aksoyoglu, M.A.; Pangeni, S.; Ashjari, M.; Brix, K.; Salluce, G.; Folgar-Cameán, Y.; Montenegro, J.; Nau, W.M. J. Am. Chem. Soc. 2023, 145, 13089–13098. c) Salluce, G.; Folgar-Cameán, Y.; Barba-Bon, A.; El Anwar, S.; Grüner, B.; Lostalé-Seijo, I.; Nau, W.M.; Montenegro, J. Angew. Chem. Int. Ed. 2024, e202404286. 

[8] Van der Meel, R.; Wender, P.A.; Merkel, O.M.; Lostalé-Seijo, I.; Montenegro, J.; Miserez, A.; Laurent, Q.; Sleiman, H.; Luciani, P. Nat. Rev. Mater. 2025, 10, 587–609. 

Dr Louis Luk, Cardiff University 

Title: Chemoenzymatic Protein Engineering with Peptide Asparaginyl Ligases (PALs) 

Late-stage modification provides a powerful route to expand protein structure and function beyond what is readily accessible through recombinant expression alone. Our work explores peptide asparaginyl ligases (PALs) as versatile biocatalytic tools for protein engineering, exploiting their ability to form peptide bonds under mild aqueous conditions and tolerate diverse synthetic substrates. In this presentation, we will highlight our efforts to enable PAL-mediated chemoenzymatic protein modification. These include driving terminal ligation towards near-complete conversion through cysteine-mediated reaction coupling. More recently, we developed a “cut–insert–ligate” strategy that recruits PAL catalysis to generate backbone-engineered proteins.