Methyl Ferulate Induced Conformational Changes of DeOxyHbS: Implication on Sickle Erythrocyte Polymerization

<p class="10-OS-Abstract">Sickle cell disease (SCD) is a molecular caused by substituting glutamic acid with valine at the β-6 position of hemoglobin, leading to polymerization erythrocytes that contain hemoglobin afterward leads severe clinical consequences. Polymerization sickle occurs only in deoxygenated form i.e deoxyhemoglobin (DeOxyHbS) polymerizes. SCD predominant children living Africa, especially West Africa. Therefore, docking and dynamic simulation studies were carried out on methyl ferulate isolated from <em>Ficus thonningii</em> leaves, known antisickling plant used Eastern Nigeria manage SCD. The Harborne procedure was for extraction, whereas combination column chromatography flash isolation purification active principles leaves extract. structure determined based nuclear magnetic resonance (NMR) analysis. A binding affinity -5.8 kcal/mol indicated binds DeOxyHbS could interfere processes trigger <em>in vitro</em>. observed variations perturbation both FTH3-DeOxyHbS complex root mean square deviation (RMSD), radius gyration (R<sub>gyr</sub>), solvent accessible surface area (SASA), potential energy (PE), Van der Waal’s (VDW) interactions obtained site amino residue performed 500 ps suggest silico residues reported being involved thus may possess potentials vitro.</p>