IIARD International Institute of Academic Research and Development

JOURNAL OF BIOLOGY AND GENETIC RESEARCH (JBGR )

E-ISSN 2545-5710
P-ISSN 2695-222X
VOL. 9 NO. 2 2023
DOI: https://doi.org/10.56201/jbgr.v9.no2.2023.pg97.107

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Impact of SDS Concentration and pH on Haemoglobin Conformation: A Comparative Spectroscopic Study

Bob Chile-Agada, Adaeze PhD

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Abstract

This study delves into the intricate interplay between Haemoglobin (Hb) and the anionic surfactant sodium dodecyl sulphate (SDS), focusing on the structural alterations induced by varying SDS concentrations (0.2mM to 1mM) at two distinct pH levels (7.2 and 5.0). Three primary objectives guide the investigation: first, to scrutinize specific structural changes in the aromatic amino region, Soret region, and oxy-band regions; second, to explore aggregations induced by SDS, emphasizing pH-dependent tendencies; and third, to characterize spectral changes, including the impact on absorbance peaks and the absorption peak at 415nm. Results reveal concentration- dependent effects of SDS on Hb conformation, with a notable disappearance of peaks at 273nm and the emergence of new peaks at 537nm. Aggregations are observed, with variations in occurrence and nature between Hb variants (AA, AS, and SS). pH-dependent responses are evident, influencing hyperchromic and hypochromic shifts, as well as the destruction or distortion of specific peaks. Comparisons between pH levels (7.2 and 5.0) demonstrate context-dependent variations in absorbance, with a distinct absorption peak at 415nm. The findings contribute biophysical insights, emphasizing the importance of understanding SDS-induced changes in protein structures. Context-specific aggregations underscore the need for nuanced control in industries where protein stability is crucial. The study's methodology enhances biophysical techniques for studying protein-surfactant interactions. Implications extend to biotechnological applications, clinical relevance, and potential avenues for future research into molecular structures. mechanisms

keywords:

Haemoglobin Conformation; Sodium Dodecyl Sulphate (SDS); Protein-Surfactant Interactions; pH-Dependent Structural Changes; Aggregation Dynamics

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References:

Aguirre-Ramírez, M., Silva-Jiménez, H., Banat, I. M., & Díaz De Rienzo, M. A. (2021).
Surfactants: physicochemical interactions with biological macromolecules. Biotechnology
Letters, 43(3), 523–535. https://doi.org/10.1007/s10529-020-03054-1.

Ahmed, M. H., Ghatge, M. S., & Safo, M. K. (2020). Haemoglobin: Structure, Function and
Allostery. Subcellular Biochemistry, 94, 345–382. https://doi.org/10.1007/978-3-030-
41769-7_14

Alresaini, S. M., Malik, A. R., Alonazi, M., Alhomida, A. S., & Khan, J. M. (2023). SDS induces
amorphous, amyloid-fibril, and alpha-helical structures in the myoglobin in a
concentration-dependent manner. International Journal of Biological Macromolecules,
231, 123237–123237. https://doi.org/10.1016/j.ijbiomac.2023.123237

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