ABSTRACT
This study explores the intricate responses of haemoglobin variants, namely HbAA, HbAS, and HbSS, to varying concentrations of hydrogen peroxide and pH conditions. Employing a rigorous purification process through ion-exchange chromatography, distinct haemoglobin variants were isolated and subjected to detailed spectroscopic analysis. The structural and functional alterations were investigated under oxidative stress induced by hydrogen peroxide, revealing variant-specific patterns in the aromatic and Soret regions. Notably, the study unveiled nuanced responses to pH changes, emphasizing the dynamic nature of haemoglobin in different environments. The lipid peroxidation determination added a layer of complexity, linking oxidative stress conditions with consequent impacts on lipid peroxidation. The findings contribute valuable insights into the broader understanding of haemoglobin’s role in oxygen transport and cellular responses to oxidative challenges. Importantly, the study sets a foundation for future investigations, shedding light on the molecular mechanisms governing haemoglobin’s adaptive responses to oxidative stress and pH fluctuations. The implications extend beyond the specific variants studied here, offering potential applications in therapeutic strategies for conditions associated with haemoglobin abnormalities and oxidative stress-related pathologies. This research underscores the multifaceted nature of haemoglobin, revealing its central role in human health and disease. The interplay of genetic, biochemical, and environmental factors explored in this study provides a comprehensive framework for advancing our understanding of haemoglobin behaviour and opens avenues for further research in clinical medicine and therapeutic interventions.
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