This study delves into the intricate interplay between sodium dodecyl Sulphate (SDS) and haemoglobin variants—HbAA, HbAS, and HbSS—with a focus on unravelling the structural and spectroscopic alterations induced by SDS at varying pH levels. Employing a range of concentrations (0.8 mM – 4 mM) of SDS, the study conducted a thorough analysis of absorbance changes in the aromatic amino region, Soret region, and oxy-band region. At pH 7.2, increasing SDS concentrations prompted a consistent decrease in absorbance, especially in the aromatic amino and Soret regions. Notable blue shifts were observed, signalling structural modifications. Complete disappearance of peaks in the oxy-band region indicated a potential compromise in oxygen-binding capacity. At pH 5.0, in addition to reduced absorbance, a novel peak emerged at 506 nm, suggesting pH-dependent conformational alterations. The study compared the effects at pH 7.2 and pH 5.0, highlighting distinct changes and indicating the influence of pH on SDS-induced denaturation. The implications of these findings are significant, uncovering the vulnerability of haemoglobin variants to SDS-induced conformational changes and the pH sensitivity of these alterations. This research contributes valuable insights into the structural dynamics of haemoglobin, particularly in the context of haemoglobinopathies. The observed spectral modifications underscore the need for a nuanced understanding of experimental conditions involving SDS and haemoglobin, guiding future research toward a more comprehensive comprehension of the molecular mechanisms at play. This study enhances the understanding of SDS-induced denaturation in haemoglobin variants, providing a foundation for further exploration into potential therapeutic interventions and diagnostic strategies in the realm of haemoglobinopathies.
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