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Investigating pH-Dependent Modulations in Haemoglobin Response to Linoleic Acid: A Spectroscopic Analysis

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Adaeze B. C.-A., Ikechukwu C.
World News of Natural Sciences
|
2024
|
vol. 53
231-243
EN
This study investigates the pH-dependent modulations in haemoglobin response to linoleic acid, employing a spectroscopic analysis across HbAA, HbAS, and HbSS variants. Concentration-dependent effects of linoleic acid at varying pH levels reveal nuanced behaviours in absorbance, peak maintenance, and spectra characteristics. At pH 7.2, HbAA and HbSS display increased absorbance with peak maintenance, while HbAS exhibits gradual absorbance rise. pH 5.0 induces absorbance increase in all variants, with maintained peaks at 415nm and gradual decrease at the oxy-band region. Variants exhibit distinct spectra characteristics, emphasizing the need for tailored approaches in clinical management. Findings align with empirical literature, emphasizing haemoglobin's multifunctionality. Implications span clinical considerations, dietary influences, and broader insights into haemoglobin stability. Suggestions for future studies propose molecular explorations, disease-specific investigations, computational modelling integration, longitudinal studies, and intervention strategy explorations. This study contributes to the evolving understanding of haemoglobin responses to environmental factors, laying groundwork for personalized approaches in healthcare and dietary recommendations.
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Investigating the Structural and Spectroscopic Changes in Haemoglobin Variants (HbAA, HbAS, and HbSS) Induced by Sodium Dodecyl Sulphate (SDS) at Varying pH Levels

100%
Chile-Agada A. B.
World News of Natural Sciences
|
2024
|
vol. 53
130-139
EN
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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