Investigation of the Effects of Various Cyclodextrins on the Stabilisation of Human Serum Albumin by a Spectroscopic Method

2015 ◽  
Vol 68 (12) ◽  
pp. 1894 ◽  
Author(s):  
Mohsen Oftadeh ◽  
Golamreza Rezaei Behbahani ◽  
Ali Akbar Saboury ◽  
Shahnaz Rafiei
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Spectroscopic Method ◽  
Phosphate Buffer Solution ◽  
Blue Shift ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Buffer Solution

The binding parameters between cyclodextrins (CDs) and human serum albumin (HSA) were investigated by isothermal titration calorimetry (ITC), fluorescence quenching, and UV-vis absorption spectroscopy at 300 K in 50 mM phosphate buffer solution. Among the various CDs investigated, β-CD has the greater ability to decrease the aggregation of HSA and the results indicated that the inhibition order is γ-CD < α-CD < β-CD. The obtained heats for HSA+CDs interactions were reported and analysed in terms of the extended solvation model, which was used to reproduce the enthalpies of HSA interactions with CDs over a broad range of complex concentrations. The binding constant and thermodynamic parameters were obtained. These suggested that the binding reaction was driven by both enthalpy and entropy, and electrostatic interactions played a major role in the stabilising of HSA. The parameters and reflected the net effect of β-CD on the HSA stability at low and high cyclodextrin concentrations, respectively. The positive values for indicated that β-CD stabilises the HSA structure at low concentrations. The UV absorption intensity of theses complexes increased and a slight red shift was observed in the absorbance wavelength with increasing the CD concentration. The fluorescence intensity of HSA decreased regularly and a slight blue shift was observed for the emission wavelength with increasing CD concentration. The results indicate that the CD complex could quench the fluorescence of HSA and changes the microenvironment of the tryptophan residue.

DENATURATION OF HUMAN SERUM ALBUMIN BY CERIUM (III) CHLORIDE

2013 ◽  
Vol 08 (01n02) ◽  
pp. 59-71
Author(s):  
G. REZAEI BEHBAHANI ◽  
M. SHALBAFAN ◽  
N. GHEIBI ◽  
L. BARZEGAR ◽  
H. REZAEI BEHBAHANI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Tertiary Structure ◽  
Fluorescence Emission ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Spectroscopic Methods ◽  
Irreversible Denaturation

Cerium (III) Chloride-induced conformational changes of human serum albumin, HSA, in phosphate buffer, 10 mM at pH 7.4 was investigated, using isothermal titration calorimetry (ITC), UV and fluorescence emission spectroscopic methods. The results indicate that CeCl3, Ce3+, induces irreversible denaturation of the HSA structure. The UV absorption intensity of HSA + Ce3+ shows a slight blueshift in the absorbance wavelength with increasing Ce3+ concentration. The fluorescence intensity was increased regularly and a slight redshift was observed in the emission wavelength. The HSA + Ce3+ complex quenches the fluorescence of HSA and changes the microenvironment of tryptophan residue. The emission intensity increases suggesting the loss of the tertiary structure of HSA. The results obtained from the ITC data are in agreement with the spectroscopic methods. The strong negative cooperativity of Ce3+ binding with HSA (Table 1) recovered from the extended solvation model, indicates that HSA has been denatured as a result of its interaction with Ce3+ ions.

Spectroscopic Studies on the Interaction between Sulfadiazine and Human Serum Albumin

2014 ◽  
Vol 1044-1045 ◽  
pp. 181-184
Author(s):  
Fang Huang ◽  
Ying Liu
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Hydrophobic Interactions ◽  
Phosphate Buffer Solution ◽  
Inner Filter Effect ◽  
Entropy Change ◽  
Spectroscopic Studies ◽  
Fluorescence Measurement ◽  
Buffer Solution

The interaction of sulfadiazine (SDZ) and human serum albumin (HSA) in phosphate buffer solution had been investigated using multi-spectroscopic methods. The inner filter effect was corrected. The quenching mechanism was determined to be static quenching according to the fluorescence measurement. The thermodynamic parameters (enthalpy change (ΔH) and entropy change (ΔS)) were calculated to be-9.70 KJ·mol-1 and 46.07 J·mol-1·K-1, respectively, which indicated that hydrogen bonds and hydrophobic interactions play the major role on driven the interaction of SDZ with HSA. SDZ binds in the vicinity of site I in HSA, and the binding distance was 1.93 nm. In addition, the effects of HSA secondary structure were quantitatively calculated by CD spectra.

Photocyclization of photoswitches with high enantioselectivity in human serum albumin in an artificial environment

2017 ◽  
Vol 53 (22) ◽  
pp. 3181-3184 ◽  
Author(s):  
Koichi Kawamura ◽  
Ken Osawa ◽  
Yuta Watanobe ◽  
Yuri Saeki ◽  
Naoki Maruyama ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Uv Irradiation ◽  
Phosphate Buffer ◽  
Enantiomeric Excess ◽  
Phosphate Buffer Solution ◽  
Ring Closure ◽  
Buffer Solution ◽  
Artificial Environment

Three photochromic bisthienylethenes exhibited 56 to >99% enantiomeric excess in photochemical ring closure upon UV irradiation when incorporated in human serum albumin dissolved in 15% acetonitrile-phosphate buffer solution and incubated for 24 h at −4 °C.

Immobilized replicates of sequence 136–148 of human serum albumin as adsorbents for bilirubin

1987 ◽  
Vol 65 (8) ◽  
pp. 1927-1934 ◽  
Author(s):  
M. Bouvier ◽  
G. R. Brown ◽  
L. E. St-Pierre
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solid Phase ◽  
Solid Phase Peptide Synthesis ◽  
Phosphate Buffer Solution ◽  
Binding Constants ◽  
Buffer Solution ◽  
A Site ◽  
Scatchard Plots

Strategic peptide sequences, patterned on the sequence 136–148 of the primary structure of human serum albumin, have been immobilized on a cross-linked polyacrylamide support using the solid phase peptide synthesis technique. Certain of the resulting materials proved to be efficient adsorbents for bilirubin from aqueous phosphate buffer solution. Amino acids such as lysine and arginine favour the binding of the ligand, whereas glutamic acid reduces it markedly. From Scatchard plots, first and second equilibrium binding constants, in the range of (0.3–9.6) × 104 M−1, were obtained using a site treatment. These binding constants are comparable to that for the binding of bilirubin by a larger fragment of bovine serum albumin that contains the synthesized sequence.

Multivariate Determination of Human Serum Albumin and γ-Globulin in a Phosphate Buffer Solution by near Infrared Spectroscopy

1998 ◽  
Vol 6 (1) ◽  
pp. 375-381 ◽  
Author(s):  
Koichi Murayama ◽  
Keiichi Yamada ◽  
Roumiana Tsenkova ◽  
Yan Wang ◽  
Yukihiro Ozaki
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Standard Error ◽  
Phosphate Buffer ◽  
Near Infrared ◽  
Phosphate Buffer Solution ◽  
Clinical Analysis ◽  
Pls Regression ◽  
Buffer Solution

Near infrared (NIR) spectra in the 1300–1850 nm region were measured for phosphate buffer solutions containing both human serum albumin and γ-globulin with various concentrations. The concentrations of albumin and γ-globulin were determined by partial least squares (PLS) regression analysis. The calibration for albumin in the concentration ranges of 0.100–8.000 g dL−1 yielded the correlation coefficient ( R) of 0.998, the standard error of calibration ( SEC) of 0.124 g dL−1, and the standard error of prediction ( SEP) of 0.152 g dL−1, respectively. Those for γ-globulin in the concentration ranges of 0.100–6.000 g dL−1 yielded were 0.998, 0.110 g dL−1 and 0.118 g dL−1, respectively. The regression coefficients ( RCs) of PLS factors for albumin were compared with those for γ-globulin. The differences were discussed for each RC between albumin and γ-globulin. The coefficient of variation ( CV) was calculated to be 0.0388 and 0.0374 for albumin and γ-globulin, respectively. The ratio of standard derivation of reference data in prediction set to SEP ( RPD) are 13.4 and 16.4 for them. These values obtained in the present study satisfy the demands of clinical analysis of blood. The present results demonstrate that it is possible to determine the concentrations of the two kinds of proteins in the solution simultaneously by use of NIR and PLS regression.

scholarly journals Human Serum Albumin Binds Native Insulin and Aggregable Insulin Fragments and Inhibits Their Aggregation

Biomolecules ◽  
2020 ◽  
Vol 10 (10) ◽  
pp. 1366 ◽  
Author(s):  
Joanna Wasko ◽  
Marian Wolszczak ◽  
Zbigniew J. Kaminski ◽  
Malgorzata Steblecka ◽  
Beata Kolesinska
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Butyric Acid ◽  
Hot Spots ◽  
Cd Spectra ◽  
Buffer Solution ◽  
Peptide Probe ◽  
Coupling Reagent ◽  
Native Insulin

The purpose of this study was to investigate whether Human Serum Albumin (HSA) can bind native human insulin and its A13–A19 and B12–B17 fragments, which are responsible for the aggregation of the whole hormone. To label the hormone and both hot spots, so that their binding positions within the HSA could be identified, 4-(1-pyrenyl)butyric acid was used as a fluorophore. Triazine coupling reagent was used to attach the 4-(1-pyrenyl)butyric acid to the N-terminus of the peptides. When attached to the peptides, the fluorophore showed extended fluorescence lifetimes in the excited state in the presence of HSA, compared to the samples in buffer solution. We also analyzed the interactions of unlabeled native insulin and its hot spots with HSA, using circular dichroism (CD), the microscale thermophoresis technique (MST), and three independent methods recommended for aggregating peptides. The CD spectra indicated increased amounts of the α-helical secondary structure in all analyzed samples after incubation. Moreover, for each of the two unlabeled hot spots, it was possible to determine the dissociation constant in the presence of HSA, as 14.4 µM (A13–A19) and 246 nM (B12–B17). Congo Red, Thioflavin T, and microscopy assays revealed significant differences between typical amyloids formed by the native hormone or its hot-spots and the secondary structures formed by the complexes of HSA with insulin and A13–A19 and B12–B17 fragments. All results show that the tested peptide-probe conjugates and their unlabeled analogues interact with HSA, which inhibits their aggregation.

scholarly journals Insight of the Interaction between 2,4-thiazolidinedione and Human Serum Albumin: A Spectroscopic, Thermodynamic and Molecular Docking Study

2019 ◽  
Vol 20 (11) ◽  
pp. 2727 ◽  
Author(s):  
Safikur Rahman ◽  
Md Tabish Rehman ◽  
Gulam Rabbani ◽  
Parvez Khan ◽  
Mohamed F AlAjmi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Study ◽  
Dynamics Simulation ◽  
Titration Calorimetry ◽  
Peroxisome Proliferator ◽  
Molecular Docking Study ◽  
Fluorescence Studies

Thiazolidinedione derivatives (TZDs) have attracted attention because of their pharmacological effects. For example, certain TZDs have been reported to ameliorate type II diabetes by binding and activating PPARs (peroxisome proliferator-activated receptors). Nonetheless, no information is available on the interaction between the heterocyclic 2, 4-thiazolidinedione (2,4-TZD) moiety and serum albumin, which could affect the pharmacokinetics and pharmacodynamics of TZDs. In this study, we investigated the binding of 2,4-TZD to human serum albumin (HSA). Intrinsic fluorescence spectroscopy revealed a 1:1 binding stoichiometry between 2,4-TZD and HSA with a binding constant (Kb) of 1.69 ± 0.15 × 103 M−1 at 298 K. Isothermal titration calorimetry studies showed that 2,4-TZD/HSA binding was an exothermic and spontaneous reaction. Molecular docking analysis revealed that 2,4-TZD binds to HSA subdomain IB and that the complex formed is stabilized by van der Waal’s interactions and hydrogen bonds. Molecular dynamics simulation confirmed the stability of the HSA-TZD complex. Further, circular dichroism and 3D fluorescence studies showed that the global conformation of HSA was slightly altered by 2,4-TZD binding, enhancing its stability. The results obtained herein further help in understanding the pharmacokinetic properties of thiazolidinedione.

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