Spin-labeled hydrogels for cell viability assessment by EPR

Vesković, Ana; Nakarada, Đura; Popović‐Bijelić, Ana

doi:10.1016/j.freeradbiomed.2021.08.084

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“…The successful use of spin-labeled albumin hydrogels for EPR characterization of ligand binding and release, protein matrix degradation, and the rate of ligand diffusion from the hydrogel water pores was demonstrated in this work. Together with our previous findings showing their applicability for cell viability assessment [95] and hydrogel water content determination [74], the role of state-of-the-art EPR for biomedical applications is emphasized, particularly in cancer research. Finally, the fact that the HL/HSA hydrogel did not exhibit cytotoxic activity in the Colo 205 human cancer cell line during the 72 h exposure time indicates that it acts as an efficient reservoir for the active ligand, even in the presence of living cells.…”

Section: Discussionmentioning

confidence: 60%

The Release of a Highly Cytotoxic Paullone Bearing a TEMPO Free Radical from the HSA Hydrogel: An EPR Spectroscopic Characterization

et al. 2022

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This study shows the potential of a thermally induced human serum albumin (HSA) hydrogel to serve as a drug depot for sustained release of a highly cytotoxic modified paullone ligand bearing a TEMPO free radical (HL). The binding of HL to HSA was studied by electron paramagnetic resonance (EPR) spectroscopy and imaging. The EPR protocol was also implemented for the study of matrix degradation, and ligand diffusion rate, in two additional spin-labeled hydrogels, containing 5-doxylstearate and 3-carbamoyl-proxyl. The results showed that the hydrogel is an efficient HL reservoir as it retained 60% of the ligand during 11 days of dialysis in physiological saline. Furthermore, upon incubation with Colo 205 human colon adenocarcinoma cells for 3 days, the HL/HSA hydrogel did not exhibit cytotoxic activity, demonstrating that it is also an efficient ligand depot in the presence of living cells. It was observed that the percentage of HL release is independent of its initial concentration in the hydrogel, suggesting that HSA possesses a specific binding site for the ligand, most likely Sudlow site 2, as predicted by molecular docking. The intrinsic property of albumin to bind and transport various substances, including hydrophobic drugs, may be fine-tuned by appropriate physical/chemical hydrogel preparation procedures, providing optimal drug delivery.

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Section: Discussionmentioning

confidence: 60%