Abstract
Transferrin belongs to a class of monomeric glycoproteins, which sequestrate and transport iron inside the body. Apart from iron, transferrin binds with various other metal ions and is assumed to deliver medicinally important metal ions to cells. Hence, the investigation of binding characteristics may provide crucial information for new drug developments. To study the biological impacts of medicinally important metal ions, in this work, we explored the binding behavior of Rh(III) ion with serum apo-transferrin (ApoHST) using FT-IR and UV-Vis spectroscopy. In FT-IR, interaction of Rh(III) with ApoHST was studied at three concentrations (0.25, 0.5, and 1 mM) of metal ion at different time intervals (15, 30, and 60 min). The IR spectra of Rh(III)-ApoHST coordinates revealed a marked reduction in amide I and II band intensities with alterations in band positions. The alpha-helical part of protein secondary structure reduced considerably (from 53% to 49%, 42%, and 39%), followed by an increment in beta-sheet and beta-turn components with the increasing concentrations of metal ion. Saturation level reached at 1 mM concentration of Rh(III) ion. In the UV-Vis spectroscopic study, absorption of metal ion-protein coordinates successively raised as concentration of Rh(III) ion increased. The binding constant (K) was calculated as 1.16x10(4) M-1, which showed a strong binding of the test metal ion with the protein. Upon coordination with a metal ion, the microenvironment of aromatic protein residues changed, which was detected by these spectroscopic techniques. The results revealed the existence of a significant interaction between Rh (III) ion and ApoHST. These research outcome may present new insight into the possible utilization of Rh(III) ion-based compounds in biomedicine. However, more investigations are needed to interpret the exact cellular mechanism.