Enhancement of enzyme activity by laser-induced energy propulsion of upconverting nanoparticles under near-infrared light: A comprehensive methodology for in vitro and in vivo applications

• Published in: International journal of biological macromolecules Vol. 260; no. Pt 2; p. 129343
• Main Authors: Ateş, Burhan, Ulu, Ahmet, Asiltürk, Meltem, Noma, Samir Abbas Ali, Topel, Seda Demirel, Dik, Gamze, Özhan, Onural, Bakar, Büşra, Yıldız, Azibe, Vardı, Nigar, Parlakpınar, Hakan
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-03-2024
• Subjects: Animals; Catalysis; Enzyme immobilization; Enzymes, Immobilized - chemistry; Infrared Rays; Nanoparticles - chemistry; Near-infrared (NIR) excitation; PEG-L-asparaginase; Rats; Triggered activity; Upconverting nanoparticles (UCNPs); Enzyme immobilization; Near-infrared (NIR) excitation; PEG-L-asparaginase; Triggered activity; Upconverting nanoparticles (UCNPs)
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2024.129343

If the appropriate immobilization method and carrier support are not selected, partial decreases in the activity of enzymes may occur after immobilization. Herein, to overcome this challenge, an excitation mechanism that enables energy transfer was proposed. Modified upconverting nanoparticles (UCNPs) were constructed and the important role of near-infrared (NIR) excitation in enhancing the catalytic activity of the enzyme was demonstrated. For this purpose, UCNPs were first synthesized via the hydrothermal method, functionalized with isocyanate groups, and then, PEG-L-ASNase was immobilized via covalent binding. UCNPs with and without PEG-L-ASNase were extensively characterized by different methods. These supports had immobilization yield and activity efficiency of >96 % and 78 %, respectively. Moreover, immobilized enzymes exhibited improved pH, thermal, and storage stability. In addition, they retained >65 % of their initial activity even after 20 catalytic cycles. Biochemical and histological findings did not indicate a trend of toxicity in rats due to UCNPs. Most importantly, PEG-L-ASNase activity was triggered approximately 5- and 2-fold under in vitro and in vivo conditions, respectively. Overall, it is anticipated that this pioneering work will shed new light on the realistic and promising usage of NIR-excited UCNPs for the immobilization of enzymes in expensive and extensive applications.
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•Upconverting nanoparticles (UCNPs) were designed for PEG-L-ASNase immobilization.•UCNPs had rod-shaped particles and particle size from 80.8 ± 27.2 nm.•The immobilized enzyme showed high stability and reusability.•No biochemical or histological toxicity due to UCNPs was observed in rats.•PEG-L-ASNase activity was triggered 2-fold as in vivo under NIR irradiation.