scholarly journals 2K1345 Thermal Unfolding Process of Bovine Serum Albumin by FT-IR Spectroscopy

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S130
Author(s):  
K. Murayama ◽  
S. Era ◽  
Y. Ozaki
Keyword(s):  
Bovine Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Thermal Unfolding ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

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.

A spectroscopic and molecular dynamics simulation approach towards the stabilizing effect of ammonium-based ionic liquids on bovine serum albumin

2017 ◽  
Vol 41 (19) ◽  
pp. 10712-10722 ◽  
Author(s):  
Lakkoji Satish ◽  
Sabera Millan ◽  
Krishnendu Bera ◽  
Sujata Mohapatra ◽  
Harekrushna Sahoo
Keyword(s):  
Molecular Dynamics ◽  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Dynamics Simulation ◽  
Thermal Unfolding ◽  
Simulation Approach ◽  
Stabilizing Effect ◽  
Theoretical Evidence

Experimental and theoretical evidence in support of the stabilizing effect of ammonium-based ionic liquids on thermal unfolding/refolding of bovine serum albumin is provided in this article.

scholarly journals Formation of Nanocomplexes between Carboxymethyl Inulin and Bovine Serum Albumin via pH-Induced Electrostatic Interaction

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3056 ◽  
Author(s):  
Guiying Huang ◽  
Jun Liu ◽  
Weiping Jin ◽  
Zihao Wei ◽  
Chi-Tang Ho ◽  
...  
Keyword(s):  
Sodium Chloride ◽  
Bovine Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Electrostatic Interaction ◽  
Bovine Serum ◽  
Titration Calorimetry ◽  
Food Ingredients ◽  
Enthalpy Changes ◽  
Ft Ir

As a functional polysaccharide, inulin was carboxymethylated and it formed nanocomplexes with bovine serum albumin (BSA). The success of obtaining carboxymethyl inulin (CMI) was confirmed by a combination of Fourier transform Infrared (FT-IR), Raman spectroscopy, gel permeation chromatography (GPC), and titration. The effects of pH and ionic strength on the formation of CMI/BSA nanocomplexes were investigated. Our results showed that the formation of complex coacervate (pHφ1) and dissolution of CMI/BSA insoluble complexes (pHφ2) appeared in pH near 4.85 and 2.00 respectively. FT-IR and Raman data confirmed the existence of electrostatic interaction and hydrogen bonding between CMI and BSA. The isothermal titration calorimetry (ITC) results suggested that the process of complex formation was spontaneous and exothermic. The complexation was dominated by enthalpy changes (∆Η < 0, ∆S < 0) at pH 4.00, while it was contributed by enthalpic and entropic changes (∆Η < 0, ∆S > 0) at pH 2.60. Irregularly shaped insoluble complexes and globular soluble nanocomplexes (about 150 nm) were observed in CMI/BSA complexes at pH 4.00 and 2.60 while using optical microscopy and atomic force microscopy, respectively. The sodium chloride suppression effect on CMI/BSA complexes was confirmed by the decrease of incipient pH for soluble complex formation (or pHc) and pHφ1 under different sodium chloride concentrations. This research presents a new functional system with the potential for delivering bioactive food ingredients.

SPECTROSCOPIC STUDY OF PROPOFOL BINDING TO HUMAN SERUM ALBUMIN

2010 ◽  
Vol 05 (04) ◽  
pp. 209-226 ◽  
Author(s):  
SAQER M. DARWISH
Keyword(s):  
Human Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Secondary Structure ◽  
Complex Molecules ◽  
Ft Ir ◽  
Β Sheets ◽  
Α Helix ◽  
Ft Ir Spectroscopy

The interaction of propofol and human serum albumin (HSA) has been investigated by UV-absorption, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectroscopy. Propofol has shown a strong ability to quench the intrinsic fluorescence of HSA through a static quenching procedure. The binding constant (k) is estimated at a low value of 2.55 × 103M-1at 293 K. FT-IR spectroscopy with Fourier self-deconvolution technique was used to determine the protein secondary structure in the amide regions I, II and III. The observed spectral changes of HSA-propofol complex indicate a larger intensity decrease in the absorption band of α-helix relative to that of β-sheets. This variation in intensity is related indirectly to the formation of H-bonding in the complex molecules, which accounts for the different intrinsic propensities of α-helix and β-sheets.

Bovine serum albumin adsorption on passivated porous silicon layers

2004 ◽  
Vol 82 (10) ◽  
pp. 1545-1553 ◽  
Author(s):  
L Tay ◽  
N L Rowell ◽  
D Poitras ◽  
J W Fraser ◽  
D J Lockwood ◽  
...  
Keyword(s):  
Porous Silicon ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Crystalline Silicon ◽  
Electrochemical Anodization ◽  
Undecylenic Acid ◽  
Ft Ir ◽  
Lift Off ◽  
Bsa Adsorption

Hydrogen-terminated porous silicon (pSi-H) films were fabricated through electrochemical anodization of crystalline silicon in hydrofluoric-acid-based solutions. The pSi-H surface was chemically functionalized by thermal reaction with undecylenic acid to produce an organic monolayer covalently attached to the silicon surface through Si—C bonds and bearing an acid terminal group. Bovine serum albumin (BSA) was adsorbed onto such surface-modified pSi structures. The resulting surfaces were characterized using scanning electron microscopy (SEM), reflection FT-IR spectroscopy, and ellipsometry. SEM showed that the porous films were damaged and partially lifted off the silicon substrate after a prolonged BSA adsorption. Ellipsometry analysis revealed that the BSA penetrated ∼1.3 µm into the porous structure. The film damage is likely a result of BSA anchoring itself tightly through strong electrostatic interaction with the acid-covered Si sidewalls. A change in surface tension during BSA film formation then causes the pSi layer to buckle and lift off the underlying Si substrate. FT-IR results from the undecylenic-acid-modified pSi surfaces before and after BSA adsorption showed the presence of strong characteristic amide I, II, and III vibrational bands after BSA adsorption. The surface properties of the pSi matrix and its interactions with BSA are examined in this study.Key words: ellipsometry, porous silicon, protein adsorption, surface passivation.

scholarly journals Study on the interaction of Prodigiosin with bovine serum albumin by spectroscopic methods

2012 ◽  
Vol 27 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Shu-Chao Liu ◽  
Jing Tang ◽  
Xi-Hai Zhang ◽  
Yuan-Yuan Gao ◽  
Fei Ma ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Fluorescence Spectra ◽  
Synchronous Fluorescence ◽  
Spectroscopic Methods ◽  
Amino Acid Residues ◽  
Absorption And Fluorescence Spectra ◽  
Ft Ir ◽  
Spectrum Experiment

The interaction between bovine serum albumin (BSA) and Prodigiosin (PG) was investigated by UV-vis absorption, fluorescence, synchronous fluorescence, FT-IR and circular dichroism (CD) techniques. The data of UV-vis absorption and fluorescence spectra displayed that there existed interaction between PG and aromatic amino acid residues of BSA. The synchronous fluorescence and CD spectrum experiment both showed that the secondary structure of BSA changed with addition of PG. All these results revealed that the conformation and microenvironment of BSA were changed.

FT-IR for the Soluble Complexes of Bovine Serum Albumin Reacted with Calcium Hydroxyapatites

1999 ◽  
Vol 15 (12) ◽  
pp. 1064-1069 ◽  
Author(s):  
Shen Yu-Hua ◽  
◽  
Yang Zhan-Lan ◽  
Wu Jin-Guang
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ft Ir ◽  
Soluble Complexes

scholarly journals Adsorption of bovine serum albumin onto synthetic Fe-doped geomimetic chrysotile

2015 ◽  
Vol 12 (107) ◽  
pp. 20150186 ◽  
Author(s):  
Alessio Adamiano ◽  
Isidoro Giorgio Lesci ◽  
Daniele Fabbri ◽  
Norberto Roveri
Keyword(s):  
Gas Chromatography ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Health Hazard ◽  
Random Coil ◽  
Gas Chromatography Mass Spectrometry ◽  
Gravimetric Analysis ◽  
Minute Amount ◽  
Ft Ir

Synthetic stoichiometric and Fe-doped geomimetic chrysotile nanocrystals represent a reference standard to investigate the health hazard associated with mineral asbestos fibres. Experimental evidence suggests that the generation of reactive oxygen species and other radicals, catalysed by iron ions at the fibre surface, plays an important role in asbestos-induced cytotoxicity and genotoxicity. In this study, structural modification of bovine serum albumin (BSA) adsorbed onto synthetic chrysotile doped with different amounts of Fe has been investigated by Fourier transform infrared spectroscopy (FT-IR), thermal gravimetric analysis (TGA) and analytical pyrolysis coupled with gas chromatography–mass spectrometry. FT-IR data evidenced a marked increase in disordered structures like random coil and β-turn of BSA–nanocrystal adduct with 0.52 wt% of Fe doped. The TGA profile of the BSA revealed that its interaction with the synthetic chrysotile surface was strongly affected by the substitution of Fe into the chrysotile structure. The 2,5-diketopiperazine yields, formed upon thermal degradation of the polypeptide chain (pyrolysis–gas chromatography), changed when the BSA was adsorbed on the nanofibres. In general, results suggested that minute amount (less than 1 wt%) of Fe doping in chrysotile affected the protein–nanofibre interactions, supporting the role that this element may play in asbestos toxicity. The catalytic role of iron and the consequent unfolding of protein due to the structural surface modification of nanofibres were also evaluated.

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