Synthesis, Characterization of the Mn(II) Complex of Rutin and Interactions between the Complex and Serum Albumins

2012 ◽  
Vol 549 ◽  
pp. 265-268 ◽  
Author(s):  
Hong Xia Li ◽  
Kun Jie Wang ◽  
De Yi Zhang ◽  
Yan Ping Wu ◽  
Hui Xia Feng ◽  
...  
Keyword(s):  
Serum Albumin ◽  
General Formula ◽  
Binding Sites ◽  
Binding Constants ◽  
Fluorescence Method ◽  
Serum Albumins ◽  
Thermogravimetric Analyses ◽  
Number Of Binding Sites

In this work, the complex of rutin-Mn has been synthesized. On the basis of elemental, thermogravimetric analyses, IR, the general formula of this complex, Na3Mn2•L(HCO3)3•3H2O is given. The interaction of serum albumin (BSA and HSA) with this complex has been studied by fluorescence method and the binding constants K (rutin-Mn-BSA: 3.1×108, 8.7×105; rutin-Mn-HSA: 3.3×107, 2.7×105) and the number of binding sites (rutin-Mn-BSA: 1.8, 1.2; rutin-Mn-HSA: 1.6, 1.1) has been obtained.

scholarly journals Interaction Between α-Glucosidase Inhibitor with Common Blood Proteins: A Thermodynamic and Spectroscopic Studies

2020 ◽  
Vol 32 (7) ◽  
pp. 1756-1762
Author(s):  
K.M. Sachin ◽  
Sameer A. Karpe ◽  
Man Singh ◽  
Ajaya Bhattarai
Keyword(s):  
Circular Dichroism ◽  
Serum Albumin ◽  
Binding Sites ◽  
Binding Constants ◽  
Spectroscopic Studies ◽  
Blood Proteins ◽  
Glucosidase Inhibitors ◽  
Number Of Binding Sites ◽  
Treatment Of Diabetes ◽  
Circular Dichroïsm

The interaction of an α-glucosidase inhibitors class of drug acarbose with globular proteins like bovine serum albumin (BSA), human serum albumin (HSA) and haemoglobin studied by fluorescence, circular dichroism (CD) spectroscopic methods. Acarbose is used for the treatment of diabetes mellitus type 2 and in some countries, prediabetes. The quenching constant (kq) values were calculated by using fluorescence data, higher with haemoglobin (at λext = 405 nm). It indicates the quenching process for the acarbose-haemoglobin interaction. Thus, the binding constants (kb), infers that the electrostatic, hydrogen bonding, and intermolecular interactions play an important role in the proteins, and drug interaction. The number of binding sites (n), between BSA, HSA and haemoglobin with acarbose was estimated by fluorescence data, the highest binding sites (15.55) of acarbose-haemoglobin at (λext = 405nm) indicates that the strong interaction or high quenching interaction. The interactions between BSA, HSA and haemoglobin with acarbose were confirmed by spectroscopic analysis and thermodynamic determination. The circular dichroism (CD) spectra implied the significant change in the conformation of BSA, HSA and haemoglobin upon binding with acarbose.

Study of the Interaction between Zinc Complex and Bovine Serum Albumin by Fluorescence Spectroscopy

2012 ◽  
Vol 554-556 ◽  
pp. 1678-1681 ◽  
Author(s):  
Yu Fen Liu ◽  
Hai Tao Xia ◽  
De Fu Rong
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Binding Sites ◽  
Bovine Serum ◽  
Binding Constants ◽  
Gibbs Free Energy Change ◽  
Binding Reaction ◽  
Physiological Conditions ◽  
Number Of Binding Sites

The binding reaction of Zn(II) complex [Zn(C8H10N)2Cl2] with bovine serum albumin(BSA) was studied by fluorescence spectroscopy under the simulative physiological conditions. The intrinsic fluorescence of BSA could be quenched by Zn(II) complex. The quenching mechanism was suggested as static quenching according to the Stern–Volmer equation. The binding constants Kband the number of binding sites n were calculated. The Zn(II) complex exhibit good binding propensity to bovine serum albumin having relatively high binding constant values. The thermodynamic parameters indicate that the hydrogen bonds and van der Waals forces play a major role in BSA-Zn(II) complex association. The process of binding was spontaneous, in which Gibbs free energy change (ΔG) was negative.

scholarly journals Characterization of the binding sites of the anticancer ruthenium(III) complexes KP1019 and KP1339 on human serum albumin via competition studies

2012 ◽  
Vol 18 (1) ◽  
pp. 9-17 ◽  
Author(s):  
Orsolya Dömötör ◽  
Christian G. Hartinger ◽  
Anna K. Bytzek ◽  
Tamás Kiss ◽  
Bernhard K. Keppler ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites

Binding of cadmium(II) and zinc(II) to human and dog serum albumins. An equilibrium dialysis and 113Cd-NMR study

1991 ◽  
Vol 69 (12) ◽  
pp. 809-820 ◽  
Author(s):  
William Goumakos ◽  
Jean-Pierre Laussac ◽  
Bibudhendra Sarkar
Keyword(s):  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Metal Ion ◽  
Equilibrium Dialysis ◽  
Scatchard Analysis ◽  
Serum Albumins ◽  
High Affinity ◽  
Nmr Study ◽  
Nmr Techniques

The binding of Cd(II) and Zn(II) to human serum albumin (HSA) and dog serum albumin (DSA) has been studied by equilibrium dialysis and 113Cd(II)-NMR techniques at physiological pH. Scatchard analysis of the equilibrium dialysis data indicate the presence of at least two classes of binding sites for Cd(II) and Zn(II). On analysis of the high-affinity class of sites, HSA is shown to bind 2.08 ± 0.09 (log K = 5.3 ± 0.6) and 1.07 ± 0.12 (log K = 6.4 ± 0.8) moles of Cd(II) and Zn(II) per mole of protein, respectively. DSA bound 2.02 ± 0.19 (log K = 5.1 ± 0.8), and 1.06 ± 0.15 (log K = 6.0 ± 0.2) moles of Cd(II) and Zn(II) per mole of protein, respectively. Competition studies indicate the presence of one high-affinity Cd(II) site on both HSA and DSA that is not affected by Zn(II) or Cu(II), and one high-affinity Zn(II) site on both HSA and DSA that is not affected by Cd(II) or Cu(II). 113Cadmium-HSA spectra display three resonances corresponding to three different sites of complexation. In site I, Cd(II) is most probably coordinated to two or three histidyl residues, site II to one histidyl residue and three oxygen ligands (carboxylate), while for the most upfield site III, four oxygens are likely to be involved in the binding of the metal ion. The 113Cd(II)-DSA spectra display only two resonances corresponding to two different sites of complexation. The environment around Cd(II) at sites I and II on DSA is similar to sites I and II, respectively, on HSA. No additional resonances are observed in any of these experiments and in particular in the low field region where sulfur coordination occurs. Overall, our results are consistent with the proposal that the physiologically important high-affinity Zn(II) and Cd(II) binding sites of albumins are located not at the Cu(II)-specific NH2-terminal site, but at internal sites, involving mostly nitrogen and oxygen ligands and no sulphur ligand.Key words: albumin, human serum, dog serum, cadmium, zinc, copper, NMR, equilibrium dialysis, binding.

scholarly journals Fluorescence Spectroscopy Study on the Interaction of Acetal Cleavable Anionic Surfactants and Bovine Serum Albumin

2014 ◽  
Vol 2014 ◽  
pp. 1-6 ◽  
Author(s):  
Xin Zhang ◽  
Jianhong Bian ◽  
Wenjie Zhai ◽  
Jing Dong ◽  
Huihui Liang ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Protein Separation ◽  
Anionic Surfactants ◽  
Binding Constants ◽  
Number Of Binding Sites ◽  
Hydrophobic Nature ◽  
Thermodynamic Relationship

The interactions between bovine serum albumin (BSA) and two cleavable anionic surfactants, sodium 3-[(2-nonyl-1,3-dioxolan-4-yl)methoxy]propane-1-sulfonate (SNPS) and sodium 3,3′-(2-nonyl-1,3-dioxane-5,5-diyl)bis(methylene)bis(oxy)dipropane-1-sulfonate (SNDPS), have been studied by means of fluorescence spectroscopy and thermodynamic analysis. The fluorescence of BSA is quenched via a static quenching mechanism with the addition of the surfactants. The binding constants of the surfactants and proteins have been measured, with KA(SNPS) = 8.71×104 M−1 and KA(SNDPS) = 7.08 × 104 M−1, respectively. The interaction between surfactants and BSA is mainly of hydrophobic nature, based on the number of binding sites, n[n(SNPS) = 1.57, n(SNDPS) = 1.47], and the thermodynamic relationship. These results suggest that SNPS and SNDPS could be effective protein denaturants for protein separation and analysis.

scholarly journals Study on the Interaction of Bovine Serum Albumin with Ceftriaxone and the Inhibition Effect of Zinc (II)

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Qiaoli Yue ◽  
Tongfei Shen ◽  
Changna Wang ◽  
Chaohui Gao ◽  
Jifeng Liu
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Interactions ◽  
Binding Sites ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Uv Absorption ◽  
Inhibition Effect ◽  
Bsa Binding ◽  
Number Of Binding Sites

The mechanism of the interaction between bovine serum albumin (BSA) and ceftriaxone with and without zinc (II) (Zn2+) was studied employing fluorescence, ultraviolet (UV) absorption, circular dichroism (CD), and synchronous fluorescence spectral methods. The intrinsic fluorescence of BSA was quenched by ceftriaxone in a static quenching mode, which was authenticated by Stern-Volmer calculations. The binding constant, the number of binding sites, and the thermodynamic parameters were obtained, which indicated a spontaneous and hydrophobic interaction between BSA and ceftriaxone regardless of Zn2+. Changes in UV absorption, CD, and synchronous fluorescence spectral data are due to the microenvironment of amide moieties in BSA molecules. In the BSA-ceftriaxone-Zn2+ system, Zn2+ must first interact with ceftriaxone forming a complex, which inhibits BSA binding to ceftriaxone. The present work uses spectroscopy to elucidate the mechanism behind the interaction between BSA and ceftriaxone in the presence and absence of Zn2+. The BSA and ceftriaxone complex provides a model for studying drug-protein interactions and thus may further facilitate the study of drug metabolism and transportation.

scholarly journals Characterization of the vitamin D-dependent Ca2+-binding sites in rat intestinal Golgi-enriched membrane fractions

1984 ◽  
Vol 218 (2) ◽  
pp. 347-354 ◽  
Author(s):  
J R F Walters ◽  
M M Weiser
Keyword(s):  
Vitamin D ◽  
Ionic Strength ◽  
Vitamin D Deficiency ◽  
Binding Sites ◽  
Control Diet ◽  
Specific Protein ◽  
High Affinity ◽  
Equilibrium Binding ◽  
Number Of Binding Sites

Rat intestinal Golgi-enriched membrane fractions take up Ca2+ by a vitamin D-dependent process that has been shown to recover within 15 min of repletion of vitamin D-deficient animals with intravenous 1,25-dihydroxycholecalciferol. The present paper reports studies characterizing the Ca2+-binding sites of these membrane fractions. Equilibrium binding of Ca2+ at concentrations between 5 and 400 microM showed significant decreases at all concentrations in membranes derived from vitamin D-deficient animals when compared with normal control-diet-fed animals. The predominant class of binding sites had a relatively high affinity for Ca2+ (KD approx. 3 microM). Vitamin D-deficiency did not change the affinity of this class of site, but decreased the number from 347 +/- 26 to 168 +/- 50 nmol of Ca2+ bound/mg of protein (means +/- S.D.). Mg2+ inhibited binding only at low Ca2+ concentrations, and the characteristics of this binding suggested positive co-operativity between two binding sites. Equimolar concentrations of Zn2+, La3+, Pb2+ and Mn2+ inhibited Ca2+ binding by over 50%. Increased ionic strength decreased Ca2+ binding by no more than half. Binding was maximal at pH 7.5 and half-maximal at pH 6.3. The large number of binding sites with relatively high affinity for Ca2+ suggests that it is unlikely that this binding is to any specific protein or to non-specific sites present on many proteins, and that the most likely sites are lipid molecules.

scholarly journals Interaction of the Fungicide Tebuconazole with Human Serum Albumin: A Preliminary Study

2018 ◽  
Vol 62 (2) ◽  
pp. 85-91 ◽  
Author(s):  
J. Staničová ◽  
K. Želonková ◽  
V. Verebová ◽  
B. Holečková ◽  
J. Dianovský
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Triazole Fungicides ◽  
Number Of Binding Sites ◽  
Preliminary Study ◽  
Protein Macromolecule

Abstract The interactions between the fungicide tebuconazole and human serum albumin were investigated using fluorescence and circular dichroism spectroscopies. The experimental results showed that the fluorescence quenching of the protein by the tebuconazole molecule was a result of the formation of a ligand-protein complex with a binding constant of 8.51×103 l.mol−1 and the number of binding sites in the macromolecule was close to 1. These findings demonstrated the fact that although the binding affinity of tebuconazole to the protein may be slight, it was very similar to other triazole fungicides. In addition, tebuconazole stabilized the α-helical secondary structure of the human serum albumin due to the increase of the α-content in the protein macromolecule.

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