Spectroscopic characterization of the interactions of bovine serum albumin with medicinally important metal ions: platinum (IV), iridium (III) and iron (II)

Serum albumin protein plays a key role in the transportation and distribution of bioactive species including metal ions metal-based drugs and, therefore, nature their binding could provide important insight for development new drugs. In present investigation, interactions bovine serum (BSA) with three biologically ions: Pt4+, Ir3+ Fe2+ were screened using easy-to-use cost-effective Fourier-Transform Infrared (FT-IR) Ultraviolet-Visible (UV-Vis) spectroscopic techniques. Prior to screening, allowed interact at physiological pH (7.4) spectral changes monitored upon interaction. FT-IR spectrum, position amide I band (C=O stretching) was shifted from 1652 cm–1 case free BSA 1659, 1657 1656 BSA-Pt4+, BSA-Ir3+ BSA-Fe2+ complexes, respectively. This shifting due N O atoms peptide bonds. The interaction further demonstrated by remarkable reduction intensities II bands. Secondary structure analysis revealed conformational characterized substantial decrease α-helix (11.29–27.41%) accompanied an increase β-sheet β-antiparallel contents. absorption constant concentration 280 nm successively reduced as Pt4+ increased. On other hand, complex increased test solution. constants complexes calculated be 1.55×104, 5.67×104 3.78×104 M-1, results that showed affinities order: Ir3+>Fe2+>Pt4+.