Protein-Based Nanozymes: From Design to Applications
CIC nanoGUNE Seminars
- Speaker
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Rocio López-Domene
CIC nanoGUNE - When
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2026/11/02
11:00 - Place
- CIC nanoGUNE Seminar room, Tolosa Hiribidea 76, Donostia-San Sebastian
- Host
- Mariana Medina
- Add to calendar
-
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Enzymes are essential catalysts in biological and industrial processes. However, their limited stability, high cost, and poor reusability have motivated the development of artificial enzyme-like systems. Nanozymes are nanomaterials that can mimic the catalytic activity of natural enzymes and offer interesting opportunities due to their robustness, tunability, and multifunctionality. They can be based on a wide range of materials, from inorganic nanoparticles to organic systems. In this talk, I will focus on the combination of metal-based catalytic systems with protein scaffolds, with the aim of using proteins not only to stabilize the nanomaterials, but also to provide a protein environment that can resemble that of natural enzymes. 1. López-Domene, R., et al. Adv. Funct. Mater., 33: 2301131. https://doi.org/10.1002/adfm.202301131
2. López-Domene, R., et al. Chem. Eur. J. 2024, 30, e202303254. https://doi.org/10.1002/chem.202303254
3. López-Domene, R., et al. Nanoscale 2023; 15 (42): 16959–16966. https://doi.org/10.1039/d3nr03443g
4. López-Domene, R., et al. ACS Appl. Mater. Interfaces 2026; https://doi.org/10.1021/acsami.6c10477
In this seminar, I will present my research journey from the design of protein-metal hybrid nanozymes during my PhD at CICbiomaGUNE to the use of nanozymes for the development of hydrogels during my postdoctoral research at LCPO in Bordeaux, France. I will first talk about the use of engineered protein scaffolds as templates for the synthesis and stabilization of metal nanoclusters, with a particular focus on platinum-based nanozymes showing multiple redox activities and enhanced stability compared with natural enzymes.1-3 I will then show how this approach can also be extended to commercially available proteins such as bovine serum albumin (BSA) for the stabilization of metal porphyrins.4 Focusing on hemin, the iron-containing porphyrin cofactor found in many heme enzymes, I will show how these protein-hemin hybrids can display interesting catalytic properties beyond standard enzymatic assays. In particular, the hybrid system was able to promote the oxidative coupling of N-acetyltyrosine, leading to the formation of dityrosine. We then took advantage of this reactivity at the macromolecular level, using the protein-based nanozyme to catalyze the crosslinking of hyaluronic acid-tyramine conjugates and form hydrogels with mechanical properties comparable to those obtained using natural enzymes. This seminar will show how protein-metal hybrid nanozymes can provide stable and versatile alternatives to natural enzymes, while also acting as functional catalysts for the fabrication of hydrogels. Finally, I will discuss how this research has led me towards my current postdoctoral work at CICnanoGUNE, where I am exploring the use of biohybrid catalytic materials for the development of nanorobotic systems for cancer-related applications.