scholarly journals 4-Hydroxycoumarin Derivative:N-(diphenylmethyl)-2-[(2-oxo-2H-chromen-4-yl)oxy]acetamide Interaction with Human Serum Albumin

2018 ◽  
Vol 2018 ◽  
pp. 1-14 ◽  
Author(s):  
Shanmugavel Chinnathambi ◽  
Subramani Karthikeyan ◽  
Mangaiyarkarsi Rajendiran ◽  
Kanniyappan Udayakumar ◽  
Arunkumar Manoharan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Active Sites ◽  
Entropy Change ◽  
Protein Molecule ◽  
Coumarin Derivative ◽  
Biologically Active ◽  
Computational Technique ◽  
Distribution Analysis

In this study, the interaction between the coumarin derivative:N-(diphenylmethyl)-2-[(2-oxo-2H-chromen-4-yl)oxy]acetamide, biologically active drug, and human serum albumin (HSA) was investigated by using various optical spectroscopy techniques along with the computational technique. The results of steady-state fluorescence spectroscopy show that the static quenching occurred while increasing the coumarin drug concentration into HSA. Also, the binding constant (K) and thermodynamical parameters of enthalpy change (ΔH°), entropy change (ΔS°), and Gibbs free energy change (ΔG°) were calculated at different temperatures (293 K, 298 K, and 303 K). The results are in good agreement with those of molecular docking studies, and also, the docking study was carried out to understand the hydrogen bonding and hydrophobic interaction between human serum albumin and coumarin derivative. In addition to the docking, charge distribution analysis was done to understand the internal stability of coumarin derivative active sites of human serum albumin. Further time-resolved emission spectroscopy (TRES) studies were carried out between free HSA and HSA-coumarin complex, and the result confirms the presence of the drug in the protein molecule without cytotoxicity.

Calcium ion binding to clinically relevant chemical modifications of human serum albumin

1995 ◽  
Vol 41 (11) ◽  
pp. 1654-1661 ◽  
Author(s):  
H Vorum ◽  
K Fisker ◽  
M Otagiri ◽  
A O Pedersen ◽  
U Kragh-Hansen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Calcium Binding ◽  
Equilibrium Dialysis ◽  
Thiol Group ◽  
Protein Molecule ◽  
Penicillin G ◽  
Lysine Residues

Abstract Calcium binding to glycated, penicilloylated, acetylated, and normal defatted human serum albumin as well as to mercapt- and nonmercaptalbumin was studied by equilibrium dialysis of radioactive Ca2+. Binding was quantified by five Scatchard constants [ni = 1, (i = 1-4) and n5 = 10]. Glycation resulted in increased k1- and k2-values and unchanged k3-k5-values, whereas penicilloylation increased all five association constants. The increments were greater the more pronounced the modification, and the enhancements caused by penicilloylation were, for the same degree of modification, greater than those produced by glycation. In contrast, acetylation by acetylsalicylate did not affect calcium binding. Likewise, binding to mercapt- and nonmercaptalbumin was the same, a finding showing that the thiol group of cysteine 34 is not important for calcium binding. D-Glucose and penicillin G are known to react with lysine residues of albumin, and the enhancement of binding resulting from glycation or penicilloylation is probably brought about by unspecific electrostatic effects, possibly supplemented by conformational changes of the protein molecule. The relative importance of the three domains of human serum albumin for calcium binding is discussed.

scholarly journals Fluorescence study on the interaction of human serum albumin with loureirin B

2010 ◽  
Vol 24 (5) ◽  
pp. 547-557 ◽  
Author(s):  
Xu Chen ◽  
Jia-Ming Ma ◽  
Ke-Lan Yong ◽  
Jing-Ci Lv ◽  
Xia-Bing Zhang
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Entropy Change ◽  
Enthalpy Change ◽  
Dynamic Quenching ◽  
Fluorescence Study ◽  
Loureirin B

The interaction between loureirin B (Lour B) and human serum albumin (HSA) was investigated by fluorescence and UV–vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants (KSV) 2.68×104, 3.30×104and 4.10×104l/mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distancerbetween HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra.

scholarly journals Investigation of the mechanism of binding of thiacloprid to human serum albumin using spectroscopic techniques and molecular modeling methods

2011 ◽  
Vol 25 (2) ◽  
pp. 113-122 ◽  
Author(s):  
Chuanxian Wang ◽  
Qinghua Chu ◽  
Changyun Chen ◽  
Zhao Bo
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Entropy Change ◽  
Binding Pocket ◽  
Cd Spectroscopy ◽  
Spectroscopic Techniques ◽  
Modeling Methods

Fluorescence spectroscopy, UV absorption, circular dichroism (CD) spectroscopy and molecular modeling methods were used to characterize the binding properties of thiacloprid (TL) with human serum albumin (HSA) at molecular level under physiological conditions. The fluorescence intensity of HSA decreased regularly with the gradually increasing concentration of thiacloprid. The binding constant K at three different temperatures (290, 300 and 310 K) were 3.07, 2.74 and 1.35 × 104M−1, respectively, for TL–HSA interaction have been calculated from the relevant fluorescence data. CD spectroscopic measurements have shown that the secondary structures of the protein have been changed by the interaction of thiacloprid with HSA. Furthermore, the study of molecular modeling indicated that thiacloprid could be located on the surface of the binding pocket of subdomains IIA in HSA. The hydrophobic interaction was the major acting force and there are H-bonds and electrostatic interactions between TL and HSA, which is in good agreement with the results from the experimental thermodynamic parameters (the enthalpy change ΔH0and the entropy change ΔS0were calculated to be -20.378 kJ/mol and 16.328 J/mol K according to the Van9t Hoff equation).

scholarly journals Deuteroporphyrin-albumin binding equilibrium. The effects of porphyrin self-aggregation studied for the human and the bovine proteins

1985 ◽  
Vol 229 (1) ◽  
pp. 197-203 ◽  
Author(s):  
M Rotenberg ◽  
R Margalit
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Competitive Model ◽  
Phosphate Buffered Saline ◽  
Self Aggregation

The binding equilibrium of deuteroporphyrin IX to human serum albumin and to bovine serum albumin was studied, by monitoring protein-induced changes in the porphyrin fluorescence and taking into consideration the self-aggregation of the porphyrin. To have control over the latter, the range of porphyrin concentrations was chosen to maker dimers (non-covalent) the dominant aggregate. Each protein was found to have one high-affinity site for deuteroporphyrin IX monomers, the magnitudes of the equilibrium binding constants (25 degrees C, neutral pH, phosphate-buffered saline) being 4.5 (+/- 1.5) X 10(7) M-1 and 1.7 (+/- 0.2) X 10(6) M-1 for human serum albumin and for bovine serum albumin respectively. Deuteroporphyrin IX dimers were found to bind directly to the protein, each protein binding one dimer, with high affinity. Two models are proposed for the protein-binding of porphyrin monomers and dimers in a porphyrin system having both species: a competitive model, where each protein molecule has only one binding site, which can be occupied by either a monomer or a dimer; a non-competitive model, where each protein molecule has two binding sites, one for monomers and one for dimers. On testing the fit of the data to the models, an argument can be made to favour the non-competitive model, the equilibrium binding constants of the dimers, for the non-competitive model (25 degrees C, neutral pH, phosphate-buffered saline), being: 8.0 (+/- 1.8) X 10(8) M-1 and 1.2 (+/- 0.6) X 10(7) M-1 for human serum albumin and bovine serum albumin respectively.

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.

Synthesis of conjugates of 5-halouracils with proteins using activated esters

1979 ◽  
Vol 44 (5) ◽  
pp. 1634-1641 ◽  
Author(s):  
Helmut Pischel ◽  
Antonín Holý ◽  
Günther Wagner
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Aminocaproic Acid ◽  
Protein Molecule ◽  
Activated Esters ◽  
High Yields ◽  
Uracil Derivative

1-Carboxymethyluracil (Ia) and its 5-fluoro (Ib), 5-bromo (Ic) and 5-iodo (Id) derivatives were transformed into the p-nitrophenyl esters IIa-IId by reaction with p-nitrophenol in the presence of N,N'-dicyclohexylcarbodiimide. Reaction of these compounds with ammonia or ε-aminocaproic acid afforded the corresponding 1-aminocarbonylmethyluracil (IIIa-d) and 1-N-(5-carboxypentyl)aminocarbonylmethyluracil (IVa-d) derivatives. Reaction of compounds II with human serum albumin and bovine γ-globulin at pH 9.2 gave high yields of conjugates of the type V and VI, respectively, containing 10-50 uracil derivative moieties bound to the protein molecule.

Gradual exposure of cystine side-chain residues during urea denaturation of human serum albumin

1981 ◽  
Vol 46 (1) ◽  
pp. 48-51 ◽  
Author(s):  
Josef Chmelík ◽  
Jiří Kadleček ◽  
Vítěz Kalous
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Protein Molecule ◽  
Side Chain ◽  
Urea Denaturation ◽  
Catalytic Hydrogen ◽  
Denaturation Curve

Showing the accessibility of disulfide groups in the protein molecule, the polarographic catalytic hydrogen current (Brdicka current) was employed for the investigation of the urea denaturation of human serum albumin. The stepwise character of the denaturation curve was accounted for the gradual conformational changes of the protein molecule and related increasing accessibility of cystine side-chain residues.

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