Cation modulation of hemoglobin interaction with sodium n-dodecyl sulphate (SDS) iv: magnesium modulation at pH 7.20

Charles O. Nwamba; Ferdinand C. Chilaka; Ali Akbar Moosavi-Movahedi; Charles O. Nwamba; Ferdinand C. Chilaka; Ali Akbar Moosavi-Movahedi

doi:10.3934/biophy.2016.1.146

AIMS Biophysics

2016, Volume 3, Issue 1: 146-170. doi: 10.3934/biophy.2016.1.146

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Cation modulation of hemoglobin interaction with sodium n-dodecyl sulphate (SDS) iv: magnesium modulation at pH 7.20

1.
Department of Chemistry, University of Idaho, 875 Perimeter Dr. MS 2343, Moscow ID 83844-2343, USA
2.
Department of Biochemistry, University of Nigeria, Nsukka
3.
Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran

Received: 12 January 2016 Accepted: 28 February 2016 Published: 07 March 2016

We investigate the interaction of Mg²⁺ (0–2.30 mM) and sodium n-dodecyl sulfate (SDS) with hemoglobins (Hbs) A and S at pH 7.20. SDS was used to model both membranes (0.60 mM SDS) and proteases (5.0 mM SDS). Via UV-visible spectroscopy, second derivative and difference second derivative spectroscopy, we interrogated for difference(s) in the interaction of these ligands with the proteins that can account for the HbS resistance to malaria parasite while been prone to sickling. Our results show that Mg²⁺ interaction with the proteins lowered the HbS oxygen affinity in comparison with the HbA. Additionally, [SDS]-protein interactions resulted in oxoferryl heme species formation that was prominent for the HbA and highly diminished for the HbS. [Mg²⁺] introduction to the [SDS]-protein mixture, however decreased the concentration of denatured protein species. The [Mg²⁺]-[SDS]-protein interactions suggest that while ionic or coulomb interactions for the HbA, in the presence of the surfactants, are [Mg²⁺] dependent, those of the HbS are not. Furthermore, hydrophobicity is a crucial force for the HbS interaction at neutral pH and is little-masked by ionic, electrostatic or coulombic interactions. In conclusion, at physiological pH, the Mg-SDS interaction decreased the HbS denaturation in comparison to the HbA.
- hemoglobins,
- protein folding,
- membranes,
- proteases,
- sodium n-dodecyl sulfate,
- denaturation,
- oxoferryl heme species
Citation: Charles O. Nwamba, Ferdinand C. Chilaka, Ali Akbar Moosavi-Movahedi. Cation modulation of hemoglobin interaction with sodium n-dodecyl sulphate (SDS) iv: magnesium modulation at pH 7.20[J]. AIMS Biophysics, 2016, 3(1): 146-170. doi: 10.3934/biophy.2016.1.146

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Abstract

We investigate the interaction of Mg²⁺ (0–2.30 mM) and sodium n-dodecyl sulfate (SDS) with hemoglobins (Hbs) A and S at pH 7.20. SDS was used to model both membranes (0.60 mM SDS) and proteases (5.0 mM SDS). Via UV-visible spectroscopy, second derivative and difference second derivative spectroscopy, we interrogated for difference(s) in the interaction of these ligands with the proteins that can account for the HbS resistance to malaria parasite while been prone to sickling. Our results show that Mg²⁺ interaction with the proteins lowered the HbS oxygen affinity in comparison with the HbA. Additionally, [SDS]-protein interactions resulted in oxoferryl heme species formation that was prominent for the HbA and highly diminished for the HbS. [Mg²⁺] introduction to the [SDS]-protein mixture, however decreased the concentration of denatured protein species. The [Mg²⁺]-[SDS]-protein interactions suggest that while ionic or coulomb interactions for the HbA, in the presence of the surfactants, are [Mg²⁺] dependent, those of the HbS are not. Furthermore, hydrophobicity is a crucial force for the HbS interaction at neutral pH and is little-masked by ionic, electrostatic or coulombic interactions. In conclusion, at physiological pH, the Mg-SDS interaction decreased the HbS denaturation in comparison to the HbA.

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