Seminarium CeNT (piątek, 17 kwietnia 2026): Artificial enzymes based on metal oxo-clusters: from discrete species to metal–organic frameworks
15 04 2026
Kategoria: Seminaria CeNT, Strona główna
Centrum Nowych Technologii Uniwersytetu Warszawskiego zaprasza na seminarium:
prof. Tatjana Parac-Vogt
KU Leuven, Belgia
Tytuł: Artificial enzymes based on metal oxo-clusters: from discrete species to metal–organic frameworks
Data: Friday, April 17, 2026
Czas: 12:00 (Central European Time)
Prowadzący: prof. Bartosz Trzaskowski
Seminarium odbędzie się w audytorium 00.142 w CeNT (Banacha 2C)
Abstrakt:
Effective catalysts for the controlled transformation of large, complex biomolecules remain rare and challenging to design. In particular, achieving selective protein hydrolysis through non-enzymatic catalysis is difficult, yet critically important for many modern applications in biotechnology and proteomics. In recent years, we have developed a conceptually new strategy for selective protein cleavage by combining the enzyme-like molecular recognition ability of polyoxometalates (POMs), a large family of soluble metal-oxo clusters, with the hydrolytic activity of strong Lewis acid metal cations (Zr, Hf) embedded within the POM framework. Using this approach, selective cleavage has been demonstrated across a range of proteins differing in size, structure, and charge. Building on this, we have shown that metal–organic frameworks (MOFs) based on {Zr6O8} clusters function as highly effective heterogeneous catalysts for peptide bond hydrolysis in various substrates. These MOFs exhibit excellent catalytic activity across a broad pH range, with significant rate accelerations compared to uncatalyzed reactions. Moreover, UiO-66 Zr-MOF has proven capable of catalyzing both intra- and intermolecular peptide bond formation, notably without inducing epimerization. The potential of metal-oxo clusters as nanozymes for protein hydrolysis has been further illustrated by the discrete {Zr6O8} cluster, which showed remarkable selectivity in the hydrolysis of myoglobin, cleaving exclusively at six aspartic acid residues out of 154 total residues.Together, these findings highlight that Zr(IV)-oxo cluster-based materials hold strong promise as a new class of dual-function nanozymes, capable of catalyzing both peptide bond hydrolysis and formation.
Bibliografia:
[1] Ly, H.G.T. et.al. J. Am. Chem. Soc. 2018,140, 6325. [2] Moons, J. et.al. Angew. Chem. Int. Ed. 2020, 59, 9094. [3] de Azambuja F., et.al. Acc. Chem. Res., 2021, 54, 1673. [4] de Azambuja, F.; ACS Catal., 2021, 11, 7647. [5] Wang, S. et.al. Nat. Commun. 2022, 13, 1284. [6] S. A. M. Abdelhameed, et.al. Nat. Commun., 2023, 14, 486. [7] K. Declerck, et al. J. Am. Chem. Soc., 2024, 146,11400. [8] S. Dai, et. al.
Nat. Commun., 2024, 15, 3434.[9] K. Declerck, et al. Angew. Chem. Int. Ed., 2025, e202512482. [10] C. Simms, et al. ACS Catal. 2025, 15, 14279. [10] K. Declerck, et al. 2026, Adv. Sci., e19545