ArticleInternational journal of molecular sciences2026
Gentamicin Targeting Human Hemoglobin Induces Methemoglobin Formation and Decreases Oxygen Affinity: A Molecular Mechanism of Hematologic Toxicity.
Article in International journal of molecular sciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The nephrotoxicity and ototoxicity of Gentamicin have been extensively investigated; however, whether they induce hematotoxicity remains unclear. This study aimed to explore the binding of Gentamicin to adult hemoglobin (HbA) and its toxicological implications. The effect of Gentamicin on HbA oxidation was assessed by quantifying methemoglobin (MetHb) formation via a four-wavelength spectrophotometric method, and scavenger rescue assays were employed to elucidate the oxidative mechanism. Alterations in the oxygen-carrying capacity of both HbA and RBCs were evaluated through the acquisition of oxygen equilibrium curves and oxygen dissociation assays. The binding affinity between Gentamicin and HbA was determined by surface plasmon resonance (SPR). Furthermore, the influence of Gentamicin on the secondary and tertiary structures of HbA was examined by microfluidic modulation spectroscopy (MMS) and UV-visible absorption spectroscopy, respectively. Molecular docking was employed to predict the binding sites of Gentamicin on HbA. Molecular dynamics simulations verified the stability of the binding. Gentamicin promoted HbA autoxidation, elevating MetHb levels, and reduced the oxygen affinity of HbA. Gentamicin-promoted HbA autoxidation is primarily mediated by both direct heme-pocket perturbation and H
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