Affiliation:
1. Lomonosov Moscow State University
Abstract
A lot of literature sources discuss diseases associated with the hemoglobin protein [1, 2]. In the modern world,
more than 800 million people suffer from anemia [3]. Assessing the level of hemoglobin in the circulatory
system is one of the ways to diagnose anemia. Hemoglobin protein is also a promising source of bioactive
peptides [4]. The aim of the work was to identify the reasons leading to conformation changes of this protein.
It still remains unclear what exactly causes disruption of its functionality. Human hemoglobin from Sigma
H7379 was studied in the work; all experiments were conducted on a dynamic light scattering spectrometer —
Photocor Complex. Experimental data were obtained using optical methods of static and dynamic light
scattering. The work included an analysis of the behaviour of hemoglobin protein molecules in aqueous and
aqueous-saline solutions with changes in solution parameters (pH, addition of iron chloride III). At values of
pH< (3.56±0.15) and pH> (10.4±0.2), the hemoglobin molecule underwent conformational changes, resulting
in the disintegration of the quaternary structure into αβ−dimers and individual α− and β−globules. As a
result of the study, it was found that the addition of FeCl3 to aqueous solutions of hemoglobin increases the
size and mass of scattering particles, which can be explained by the adsorption of Fe3+ ions on the protein
surface. However, upon reaching a certain concentration of FeCl3, the pH of the solution was lowered to such
an extent that it caused conformational changes in hemoglobin, leading to the disintegration of its quaternary structure. These results can be taken into account when creating medicinal drugs for the treatment of anemia
and other diseases associated with the hemoglobin protein.
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