Heat-induced secondary structural studies of human serum albumin in aqueous solutions by two-dimensional FT-IR spectroscopy

2000 ◽  
Author(s):  
Yuqing Wu
Keyword(s):  
Human Serum Albumin ◽  
Ir Spectroscopy ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Human Serum ◽  
Two Dimensional ◽  
Structural Studies ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

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.

scholarly journals Molecular mechanistic vision on binding interaction of triptan drug, a serotonin (5-HT1) agonist with human serum albumin through multispectral and computational assessments

2020 ◽  
Vol 11 (2) ◽  
pp. 145-155
Author(s):  
Manjushree Makegowda ◽  
Revanasiddappa Hosakere Doddarevanna
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Clinical Medicine ◽  
Fluorescence Emission ◽  
Binding Constants ◽  
Binding Interaction ◽  
Binding Ability ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

The triptan drug such as eletriptan in combination with hydrochloride (ETP) is a 5-HT1 receptor agonist used to treat the migraine headache. Human serum albumin (HSA), the fundamental serum protein, executes various functions, that includes transporting and binding of many ligands. HSA binding interaction with ETP is elucidated from molecular docking in composite with fluorescence (emission, 3D and synchronous), UV-vis and FT-IR spectroscopy at 296, 304 and 312 K (pH = 7.40). ETP after interaction modified the HSA secondary structure and its micro-environments. Energy transfer and thermodynamic parameters were evaluated. Various quenching and binding constants were computed for formed ETP-HSA complex. The dominant interactive forces for ETP and HSA binding are hydrogen bonds join up with van der Waals extent possibly at site III (IB). The presence of Ca2+, Co2+, Na+, Mg2+ and Fe3+ ions significantly affected binding ability of ETP towards HSA. The essentialness of this investigation is beneficial in life sciences, medicinal chemistry, pharmaceutical industry and clinical medicine.

Interaction of human serum albumin with oxovanadium ions studied by FT-IR spectroscopy and gel and capillary electrophoresis

2001 ◽  
Vol 79 (10) ◽  
pp. 1415-1421 ◽  
Author(s):  
M Purcell ◽  
J F Neault ◽  
H Malonga ◽  
H Arakawa ◽  
H A Tajmir-Riahi
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Ir Spectroscopy ◽  
Metal Ion ◽  
Binding Mode ◽  
Ion Binding ◽  
Metal Ion Binding ◽  
Ft Ir ◽  
Ft Ir Spectroscopy ◽  
Oxovanadium Compounds

Some oxovanadium compounds have shown potential to inhibit RNase activity, while at the same time not inhibiting DNase activity. Some vanadyl complexes also inhibit protein synthesis in rabbit reticulocytes, but induce activation of protein–tyrosine kinase. To gain an insight into the interaction of oxovanadium ions with proteins, the present study was designed to examine the bindings of VOSO4 and NaVO3 salts with human serum albumin (HSA) in aqueous solution at physiological pH with metal ion concentrations of 0.0001 to 1 mM and HSA (fatty acid free) concentration of 2% w/v. Gel and capillary electrophoresis (CE) and Fourier transform infrared (FT-IR) spectroscopic methods were used to determine the metal ion binding mode, association constant, and the secondary structure of the protein in the presence of the oxovanadium compounds. Gel electrophoresis results showed that a maximum of 20 vanadyl cations (VO2+) are bound per HSA molecule with strong (K1 = 7.0 × 107 M–1) and weak (K2 = 6.5 × 105 M–1) bindings. Similarly, capillary electrophoresis showed two major bindings for vanadyl cation with K1 = 1.2 × 108 M–1 and K2 = 8.5 × 105 M–1, whereas vanadate (VO–3) has only a weak binding affinity (K = 6.0 × 103 M–1) with HSA molecule. The VO–3 binds mainly to the lysine ε-amino NH+3 groups, while VO2+ binds possibly to the histidine nitrogen atom and the N-terminal of the α-amine residue. Infrared spectroscopic analysis showed metal ion binding results in major protein secondary structural changes from that of the α-helix (55.0 to 43–44%) to the β-sheet (22.0 to 23–26%), β-antiparallel (12.0 to 13–16%), and turn (11.0 to 17–18%), at high metal ion concentration. The observed spectral changes indicate a partial unfolding of the protein structure, in the presence of oxovanadium ions.Key words: oxovanadium, protein, binding mode, binding constant, secondary structure, electrophoresis, FT-IR spectroscopy.

Light-Induced Two-Dimensional FT-IR Spectroscopy of BacterioRhodopsin

2000 ◽  
Vol 54 (11) ◽  
pp. 1659-1664 ◽  
Author(s):  
P. G. H. Kosters ◽  
A. H. B. de Vries ◽  
R. P. H. Kooyman
Keyword(s):  
Ir Spectroscopy ◽  
Two Dimensional ◽  
Ft Ir ◽  
Ft Ir Spectroscopy

Two-Dimensional Attenuated Total Reflection/Infrared Correlation Spectroscopy Studies on Concentration and Heat-Induced Structural Changes of Human Serum Albumin in Aqueous Solutions

2002 ◽  
Vol 56 (9) ◽  
pp. 1186-1193 ◽  
Author(s):  
Yuqing Wu ◽  
Koichi Murayama ◽  
Boguslawa Czarnik-Matusewicz ◽  
Yukihiro Ozaki
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Ir Spectra ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Correlation Spectroscopy ◽  
Random Coil ◽  
Two Dimensional

Attenuated total reflection (ATR)/FT-IR spectra were measured for human serum albumin (HSA) in aqueous solutions (pH 6.6) with concentrations of 1.0, 2.0, 3.0, 4.0, and 5.0 wt % over a temperature range of 45–80 °C. Generalized two-dimensional (2D) correlation spectroscopy was employed to explore concentration and heat-induced structural variations of HSA in aqueous solutions. To generate 2D correlation spectra, the raw spectra were subjected to the appropriate pretreatment procedure involving ATR correction, subtraction of the spectrum of an aqueous solution, and smoothing. The synchronous and asynchronous correlation spectra were calculated for the concentration-dependent IR spectral variations in the amide I region at various temperatures. The two-dimensional ATR/IR correlation spectra greatly enhance band separation in the region and provide information about the correlation between the amide bands of HSA arising from the same and different secondary structure components. Based on the correlation investigated and previously proposed relationship between the secondary structure elements and the amide band frequencies, we have proposed the detailed assignments in the amide I region at 45 and 80 °C. The proposed assignments are compared with those based on the results of second derivative and Fourier self-deconvolution (FSD) of the ATR/IR spectra. The asynchronous spectrum generated from the concentration-dependent spectral variations at 45 °C show that side chains, the random coil, and extended chains are more sensitive than the α-helices and β-turns to the concentration change. On the other hand, the corresponding spectrum at 80 °C reveals that the conformation changes in side chains and β-turns (or β-strands) of HSA start before those in extended chain, random coil structures, and α-helices.

scholarly journals Calculation of the Effective Macromolecular Radii of Human Serum Albumin from the Shear Viscosity Data for Its Aqueous Solutions

2019 ◽  
Vol 64 (4) ◽  
pp. 287 ◽  
Author(s):  
O. V. Khorolskyi
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Human Serum ◽  
Shear Viscosity ◽  
Effective Radius ◽  
Water Molecules ◽  
Viscosity Data ◽  
Molecular Radius

The Malomuzh–Orlov theory is used to analyze the experimental shear viscosity data obtained for aqueous solutions of human serum albumin (HSA) at pH = 7.0 in wide temperature and concentration intervals, which allowed the effective radii of HSA macromolecules to be calculated. It is shown that three intervals of the effective molecular radius of HSA with different behaviors can be distinguished in a temperature interval of 278–318 K: 1) below the crossover concentration, the effective molecular radius of HSA remains constant; 2) in the interval from the crossover concentration to about 10 wt%, the effective molecular radius of HSA in the aqueous solution nonlinearly decreases; and 3) at concentrations of 10.2–23.8 wt%, the effective radius of HSA macromolecules linearly decreases, as the concentration grows. The assumption is made that the properties of water molecules in the solution bulk play a crucial role in the dynamics of HSA macromolecules at the vital concentrations of HSA in the solutions. The role of water near the surface of HSA macromolecules and the corresponding changes of its physical properties have been discussed.

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