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

Abstract

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

One-Pot Surface Modification of β-Cu2O NPs for Biocatalytic Performance against A-549 Lung Carcinoma Cell Lines through Docking Analysis

“…l -Ascorbic acid (LAA) transports various substances like bilirubin, fatty acids, metal ions, hormones, and exogenous drugs and functions mainly as a carrier protein for steroid and thyroid hormones that play a major role in stabilizing extracellular fluid volume by contributing to the oncotic pressure (colloid osmotic pressure) of plasma and in a class of mammals with diverse functions in the transportation of substances and the metabolism and distribution of exogenous and endogenous molecules . Bovine serum albumin (BSA) is mainly selected as an adequate protein model for drug–protein interaction due to its low cost, availability, morphological resemblance with human serum albumin, and high bonding sites to metal complexes …”

Binding Investigation of Some Important Metal Ions Copper (I), Nickel (II), and Aluminium (III) with Bovine Serum Albumin Using Valid Spectroscopic Techniques

“…To measure the extent of interaction of metal ions with the BSA protein, binding constants were calculated for the BSA-Cu+, BSA-Ni +2 , and BSA-Al +3 complexes and were found to be 3.46 × 10 4 M −1 , 1.28 × 10 4 M −1 , and 2.08 × 10 4 M −1 , respectively (Figures 5(a)-5(c)). As reported earlier, the ideal binding constant should be between 10 4 and 10 6 M −1 [1], and the ligands with their binding constant values in this range are believed to be suitable for drug development. As the metal ions also showed binding constants in this range, they and their metal-based ligands are expected to efectively bind to the BSA protein and distribute themselves throughout the biological system.…”

“…Albumin, the most prevalent plasma protein, accounts for almost 60% of the total plasma protein content in vertebrates. Owing to its widespread accessibility and similarity (76%) with human serum albumin (HSA), bovine serum albumin (BSA) is widely used to investigate the binding of biologically active molecules to the albumin protein [1]. Te BSA protein molecule is made up of a single chain consisting of 583 amino acids bonded together with 17 cysteine residues and has a molecular weight of 66400 Da.…”

Au@bovine serum albumin nanoparticle-based acid-resistant nanozyme quartz crystal microbalance sensing of urine glucose

“…2(b) . 24 Accordingly, the color of the mixed solution changed from colorless to purple. Furthermore, the results of ICP-MS and TGA show that the Au mass fraction is about 24% in Au@BSA-10 NPs.…”