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In vitro studies of hemoglobin's affinity for the Vitamin B9 and control of its stability character

Katarzyna Wiglusz1, Ewa Żurawska-Płaksej2, Agnieszka Piwowar2

  • 1Department of Basic Chemical Sciences, Faculty of Pharmacy, Wroclaw Medical University, Borowska 211 A, 50556 Wroclaw, Poland.

International Journal of Biological Macromolecules
|May 29, 2024
PubMed

Vitamin B9, known as folic acid, and hemoglobin play an important biological role in the human body. This study was designed to investigate the nature of the complex through multispectroscopic methods at physiological conditions due to the lack of research on the binding interactions between folic acid and hemoglobin. Structural analysis showed that the interactions between the molecules are mainly hydrophobic with binding constant of 0.73 × 104 L/mol at 37 °C. The secondary structure of the protein was stable after the addition of folic acid with a 20-fold excess of ligand per mol protein. The stability effect of folic acid on hemoglobin was examined as a function of release of iron ions and determination of the level of phenanthroline-Fe2+ complex. The protective function of folic acid was observed at a concentration of 6.12 nmol/L, and the release of iron ions was lower than in the control probe.

Keywords:
Drug-protein binding by spectroscopic methodsRelease iron ions from hemoglobinVitamin B9

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