scholarly journals FT-IR Spectroscopy for the Identification of Binding Sites and Measurements of the Binding Interactions of Important Metal Ions with Bovine Serum Albumin

2019 ◽  
Vol 87 (1) ◽  
pp. 5 ◽  
Author(s):  
Hassan Alhazmi
Keyword(s):  
Bovine Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Metal Ion ◽  
Binding Interaction ◽  
Binding Interactions ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Proteins play crucial roles in the transportation and distribution of therapeutic substances, including metal ions in living systems. Some metal ions can strongly associate, while others show low affinity towards proteins. Consequently, in the present work, the binding behaviors of Ca2+, Ba2+, Ag+, Ru3+, Cu2+ and Co2+ with bovine serum albumin (BSA) were screened. BSA and the metal ions were allowed to interact at physiological pH and their binding interactions were screened by using FT-IR spectroscopy. Spectra were collected by using hydrated films over a range of 4000–400 cm−1. The interaction was demonstrated by a significant reduction in the spectral intensities of the amide I (C=O stretching) and amide II bands (C–N stretching coupled to NH bending) of the protein after complexation with metal ions. The binding interaction was further revealed by spectral shifting of the amide I band from 1651 cm−1 (free BSA) to 1653, 1654, 1649, 1655, 1655, and 1654 cm−1 for BSA–Ca2+, BSA–Ba2+, BSA–Ag+, BSA–Ru3+, BSA–Cu2+ and BSA–Co2+ complexes, respectively. The shifting of the amide I band was due to the interactions of metal ions with the O and N atoms of the ligand protein. Estimation of the secondary protein structure showed alteration in the protein conformation, characterized by a marked decrease (12.9–40.3%) in the α-helix accompanied by increased β-sheet and β-turn after interaction with the metal ions. The interaction results of this study were comparable with those reported in our previous investigation of metal ion–BSA interactions using affinity capillary electrophoresis (ACE), which has proven the accuracy of the FT-IR technique in the measurement of interactions between proteins and metal ions.

scholarly journals Molecular docking and multitudinous spectroscopic studies to elucidating proton-pump inhibitor a lansoprazole binding interaction with bovine serum albumin

2019 ◽  
Vol 9 (4) ◽  
pp. 4015-4021
Keyword(s):  
Proton Pump Inhibitor ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Proton Pump ◽  
Bovine Serum ◽  
Fluorescence Emission ◽  
Spectroscopic Studies ◽  
Binding Interaction ◽  
Ft Ir ◽  
Bsa Interaction

A carrier protein called bovine serum albumin (BSA) interaction with proton-pump inhibitor such as lansoprazole (LSE) has been investigated at 295, 303 and 311 K in pH 7.40 by docking and [UV–vis, CD, FT–IR and fluorescence (emission, 3D and synchronous)] spectroscopic studies. Emission fluorescence has suggested LSE BSA complex formation by static quenching with strong binding. This interaction has proceeded by Vander Waals and hydrogen bonding. An observation from competitive site marker and docking experiments has resulted in binding of LSE with BSA transpired at site II, whereas from Förster’s theory a binding distance ( ) was retrieved to be 0.19 Å from LSE to Trp of BSA. Change in conformation, secondary structure and microenvironment of BSA were noticed after LSE interaction. Diminished binding constant in Zn2+, Na+, Fe2+, Ca2+ and Co2+ ions presence on LSE-BSA interaction was also identified.

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

2021 ◽  
Author(s):  
Hassan A Alhazmi ◽  
Mohammed Al Bratty ◽  
Abdulkarim M. Meraya ◽  
Asim Najmi ◽  
Md Shamsher Alam ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Spectroscopic Characterization ◽  
New Drugs ◽  
Spectroscopic Techniques ◽  
Protein Structure Analysis ◽  
Ft Ir

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+.

scholarly journals A Diversified Spectrometric and Molecular Docking Technique to Biophysical Study of Interaction between Bovine Serum Albumin and Sodium Salt of Risedronic Acid, a Bisphosphonate for Skeletal Disorders

2018 ◽  
Vol 2018 ◽  
pp. 1-13 ◽  
Author(s):  
M. Manjushree ◽  
Hosakere D. Revanasiddappa
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Salt ◽  
Bovine Serum ◽  
Biologically Active ◽  
Risedronic Acid ◽  
Binding Interaction ◽  
Vis Spectroscopy ◽  
Ft Ir

The binding interaction between bovine serum albumin (BSA) and sodium salt of risedronic acid (RSN) was studied by using the FT-IR (Fourier transform infrared), UV-Vis (ultraviolet–visible), fluorescence (emission and synchronous), CD (circular dichroism) spectrometric, and computational (molecular docking) techniques at 289, 297, and 305 K temperatures with physiological buffer of pH 7.40. The conformational and secondary structural changes observed for BSA from CD spectra and by curve fitting procedure were applied to Fourier self-deconvolution in FT-IR spectra. The formation of a BSA-RSN complex was confirmed from UV-Vis spectroscopy. The static type of quenching shown for RSN to BSA was verified from Stern–Volmer and modified Stern–Volmer equations. The binding constant of order 105 was obtained to be confirming that there exists a strong binding interaction between BSA and RSN. Synchronous fluorescence shows that the microenvironment of tryptophan was altered, not tyrosine of BSA; in addition to this, the distance between tryptophan of BSA and RSN was found out from Forster’s theory of nonradiation energy transfer. The interaction between BSA and RSN mainly occurred as a result of hydrogen bonds and van der Waals forces, the process is exothermic and spontaneous, and it was achieved through van ’t Hoff equation. This interaction was affected by the presence of biologically active Fe2+, Ni2+, Ca2+, Mg2+, and Cd2+ ions and was also studied. The subdomain IIIA of BSA involved with RSN interaction was authenticated from molecular docking analysis.

scholarly journals Molecular Docking and Extended Spectroscopy to Binding Characterizations: Etoposide a Glycoside of Podophyllotoxin with Bovine Serum Albumin

2021 ◽  
Vol 12 (1) ◽  
pp. 264-278
Keyword(s):  
Drug Delivery ◽  
Energy Transfer ◽  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Discovery Process ◽  
Binding Interaction ◽  
Bsa Binding ◽  
Ft Ir

A significant soluble protein, specifically bovine serum albumin (BSA) plays an efficient role in drug delivery, and etoposide (ETS) is used to cure various cancers. Binding interaction between ETS and BSA examined by 3D, emission, synchronous fluorescence’s, UV–vis, FT–IR, and CD spectroscopy’s in the association of computational at pH 7.40 with 293, 301 and 309 K. Formed complex between ETS and BSA dominates van der Waals and bonding of hydrogen’s at sub-domain IIIA. Strong binding of ETS-BSA leads to altering BSA’s structural and conformations statically. Energy transfer reveals ETS-BSA distance. Apart from this, ETS-BSA binding is affected by Mg2+, Cu2+, Fe2+, Ca2+, and Co2+ ions. This study may help in the drug development and discovery process.

FT-IR Spectroscopy As A Tool For The Study Of Metal Ions/D- Galactose Complexes

1989 ◽  
Author(s):  
Ning Xi ◽  
Shifu Weng ◽  
Jinguang Wu ◽  
Guangxian Xu
Keyword(s):  
Ir Spectroscopy ◽  
Metal Ions ◽  
Ft Ir ◽  
Ft Ir Spectroscopy
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