TY  - JOUR
AU  - Andrys, Rudolf
AU  - Monnier, Charline
AU  - Antonijević-Miljaković, Evica
AU  - Mickova, Veronika
AU  - Musilek, Kamil
AU  - Zemanova, Lucie
PY  - 2024
UR  - https://farfar.pharmacy.bg.ac.rs/handle/123456789/5643
AB  - Enzyme handling and utilization bears many challenges such as their limited stability, intolerance of organic solvents, high cost, or inability to reuse. Most of these limitations can be overcome by enzyme immobilization on the surface of solid support. In this work, the recombinant form of human cholinesterases and monoamine oxidases as important drug targets for neurological diseases were immobilized on the surface of magnetic non-porous microparticles by a non-covalent bond utilizing the interaction between a His-tag terminus on the recombinant enzymes and cobalt (Co2+) ions immobilized on the magnetic microparticles. This type of binding led to targeted enzyme orientation, which completely preserved the catalytic activity and allowed high reproducibility of immobilization. In comparison with free enzymes, the immobilized enzymes showed exceptional stability in time and the possibility of repeated use. Relevant Km, Vmax, and IC50 values using known inhibitors were obtained using particular immobilized enzymes. Such immobilized enzymes on magnetic particles could serve as an excellent tool for a sustainable approach in the early stage of drug discovery.
PB  - Elsevier B.V.
T2  - Talanta
T1  - Towards cost-effective drug discovery: Reusable immobilized enzymes for neurological disease research
VL  - 276
DO  - 10.1016/j.talanta.2024.126263
ER  - 

@article{
author = "Andrys, Rudolf and Monnier, Charline and Antonijević-Miljaković, Evica and Mickova, Veronika and Musilek, Kamil and Zemanova, Lucie",
year = "2024",
abstract = "Enzyme handling and utilization bears many challenges such as their limited stability, intolerance of organic solvents, high cost, or inability to reuse. Most of these limitations can be overcome by enzyme immobilization on the surface of solid support. In this work, the recombinant form of human cholinesterases and monoamine oxidases as important drug targets for neurological diseases were immobilized on the surface of magnetic non-porous microparticles by a non-covalent bond utilizing the interaction between a His-tag terminus on the recombinant enzymes and cobalt (Co2+) ions immobilized on the magnetic microparticles. This type of binding led to targeted enzyme orientation, which completely preserved the catalytic activity and allowed high reproducibility of immobilization. In comparison with free enzymes, the immobilized enzymes showed exceptional stability in time and the possibility of repeated use. Relevant Km, Vmax, and IC50 values using known inhibitors were obtained using particular immobilized enzymes. Such immobilized enzymes on magnetic particles could serve as an excellent tool for a sustainable approach in the early stage of drug discovery.",
publisher = "Elsevier B.V.",
journal = "Talanta",
title = "Towards cost-effective drug discovery: Reusable immobilized enzymes for neurological disease research",
volume = "276",
doi = "10.1016/j.talanta.2024.126263"
}

Andrys, R., Monnier, C., Antonijević-Miljaković, E., Mickova, V., Musilek, K.,& Zemanova, L.. (2024). Towards cost-effective drug discovery: Reusable immobilized enzymes for neurological disease research. in Talanta
Elsevier B.V.., 276.
https://doi.org/10.1016/j.talanta.2024.126263

Andrys R, Monnier C, Antonijević-Miljaković E, Mickova V, Musilek K, Zemanova L. Towards cost-effective drug discovery: Reusable immobilized enzymes for neurological disease research. in Talanta. 2024;276.
doi:10.1016/j.talanta.2024.126263 .

Andrys, Rudolf, Monnier, Charline, Antonijević-Miljaković, Evica, Mickova, Veronika, Musilek, Kamil, Zemanova, Lucie, "Towards cost-effective drug discovery: Reusable immobilized enzymes for neurological disease research" in Talanta, 276 (2024),
https://doi.org/10.1016/j.talanta.2024.126263 . .