TOXICITY OF HEMOGLOBIN DERIVATIZED WITH OXIDIZED ADENOSINE TRIPHOSPHATE AGAINST TUMORAL HUMAN CELLS

Eva  FISCHER-FODOR; Kinga  SZABO; Florina  SCURTU; Maria  LEHENE; Radu  SILAGHI-DUMITRESCU

doi:10.24193/subbchem.2023.3.10

TOXICITY OF HEMOGLOBIN DERIVATIZED WITH OXIDIZED ADENOSINE TRIPHOSPHATE AGAINST TUMORAL HUMAN CELLS

Authors

Eva FISCHER-FODOR Department for Tumor Biology, Comprehensive Cancer Center, “Prof. Dr. Ion Chiricuta” Institute of Oncology, Cluj-Napoca, Romania. Email: fischer.eva@iocn.ro. https://orcid.org/0000-0002-0898-0547
Kinga SZABO Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University, Cluj-Napoca, Romania. Email: kinga.szabo@ubbcluj.ro.
Florina SCURTU Department of Chemistry and Chemical Engineering, Babeş-Bolyai University, Cluj-Napoca, Romania. Email: florinadeac@chem.ubbcluj.ro. https://orcid.org/0000-0002-2406-9163
Maria LEHENE Faculty of Chemistry and Chemical Engineering, Babeş-Bolyai University, Cluj-Napoca, Romania. Corresponding author: radu.silaghi@ubbcluj.ro. https://orcid.org/0000-0003-0768-2342
Radu SILAGHI-DUMITRESCU Department of Chemistry and Chemical Engineering, Babes-Bolyai University, Cluj-Napoca; Romanian Chemical Society, Romanian Society of Biochemistry and Molecular Biology, Society of Biological Inorganic Chemistry, Romania. Email: radu.silaghi@ubbcluj.ro. https://orcid.org/0000-0003-3038-7747

DOI:

https://doi.org/10.24193/subbchem.2023.3.10

Keywords:

hemoglobin, cells, oATP, blood substitute, cancer

Abstract

Adenosine triphosphate (ATP) has a high affinity for the organic phosphate binding site of hemoglobin (Hb), affecting the affinity for oxygen. Periodate-oxidized-ATP (oATP) behaves as an affinity tag for several enzymes that use ATP as a substrate and has the ability to form intermolecular aldimine bonds by reaction with free amino groups on proteins. Due to its unique structure, oATP has been used to produce structural and functional modifications of Hb to obtain a compound with a low affinity for oxygen that could be used as a blood substitute. However, the oATP-Hb derivative was shown to present a notable increase in pro-oxidative reactivity compared to Hb in vitro, and accordingly exhibited toxicity in in vivo studies. This pro-oxidant reactivity was alleviated by crosslinking Hb with bovine serum albumin (BSA) in an oATP-Hb-BSA copolymer. We now show that oATP and oATP-Hb-BSA display high-affinity toxicity towards cancer cells, and may hence deserve further investigation as adjuvants in anti-cancer therapy.

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STUDIA UBB CHEMIA, Volume 68 (LXXVIII), No. 3, September 2023

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Published

2023-09-25

How to Cite

FISCHER-FODOR, E. ., SZABO, K. ., SCURTU, F. ., LEHENE, M. ., & SILAGHI-DUMITRESCU, R. . (2023). TOXICITY OF HEMOGLOBIN DERIVATIZED WITH OXIDIZED ADENOSINE TRIPHOSPHATE AGAINST TUMORAL HUMAN CELLS. Studia Universitatis Babeș-Bolyai Chemia, 68(3), 153–160. https://doi.org/10.24193/subbchem.2023.3.10