A DSC study of zinc binding to bovine serum albumin (BSA)

The thermal denaturation of bovine serum albumin (BSA) is a kinetically and thermodynamically controlled process. The effects of zinc binding to bovine serum albumin (BSA), followed by differential scanning calorimetry (DSC), were investigated in this work, with the purpose of obtaining a better understanding of the albumin/zinc interaction. From the DSC curves, the thermodynamic parameters of protein denaturation were obtained, i.e., the temperature of thermal transition maximum (T m), calorimetric enthalpy (?Hcal), van't Hoff enthalpy (?HvH), the number of binding sites (I, II), the binding constants for each binding site (K bI, K bII) and the average number of ligands bound per mole of native protein X N. The thermodynamic data of protein unfolding showed that zinc binding to bovine serum albumin increases the stability of the protein (higher values of ?Hcal) and the different ratio ?Hcal/?HvH indicates the perturbation of the protein during thermal denaturation.

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Influence of complex formation with tetraantraquinoporphyrazines and tetrasulphophthalocyanine on thermal stability of bovine serum albumin

Journal of Porphyrins and Phthalocyanines ◽

10.1142/s1088424611003185 ◽

2011 ◽

Vol 15 (04) ◽

pp. 223-229 ◽

Cited By ~ 6

Author(s):

Natalia Lebedeva ◽

Tatyana Popova ◽

Malgorzata Kozbial ◽

Malgorzata Wszelaka-Rylik ◽

Yuri Gubarev ◽

...

Keyword(s):

Thermal Stability ◽

Differential Scanning Calorimetry ◽

Bovine Serum Albumin ◽

Complex Formation ◽

Serum Albumin ◽

Bovine Serum ◽

Thermal Denaturation ◽

Scanning Calorimetry ◽

Electron Absorption Spectroscopy ◽

Thermal Stability Of

Interaction between bovine serum albumin (BSA) and tetraantraquinoporphyrazines (TAP) and tetrasulphophthalocyanine (Pc) aluminum hydroxide was studied by means of electron absorption spectroscopy, IR spectroscopy, fluorescence spectroscopy and differential scanning calorimetry. It was found that the complex formation of BSA with the TAPs results in increase of thermal stability of the protein while Pc does not have remarkable influence on the protein thermal denaturation.

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Effect of the degree of glycation on the stability and aggregation of bovine serum albumin

Food Hydrocolloids ◽

10.1016/j.foodhyd.2020.105892 ◽

2020 ◽

Vol 106 ◽

pp. 105892 ◽

Cited By ~ 2

Author(s):

Xuanting Liu ◽

Jingbo Liu ◽

Wenqi Zhang ◽

Robin Pearce ◽

Meiru Chen ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

The Stability

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Investigating the Size-Dependent Binding of Pristine nC60 to Bovine Serum Albumin by Multi-Spectroscopic Techniques

Materials ◽

10.3390/ma14020298 ◽

2021 ◽

Vol 14 (2) ◽

pp. 298

Author(s):

Shufang Liu ◽

Shu’e Wang ◽

Zhanzuo Liu

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Binding Constants ◽

Inner Filter Effect ◽

Spectroscopic Techniques ◽

Size Distributions ◽

Size Dependent ◽

Filter Effect ◽

Vis Spectroscopy

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

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The Properties of Polyesteramide and the Effects on the Stability of Bovine Serum Albumin

Pharmaceutical Development and Technology ◽

10.1080/10837459908984229 ◽

1999 ◽

Vol 4 (1) ◽

pp. 97-106 ◽

Cited By ~ 3

Author(s):

Wei Ping Ye ◽

Yong Xu ◽

Fu Sheng Du

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

The Stability

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Ketoprofen-Based Ionic Liquids: Synthesis and Interactions with Bovine Serum Albumin

Molecules ◽

10.3390/molecules25010090 ◽

2019 ◽

Vol 25 (1) ◽

pp. 90 ◽

Cited By ~ 3

Author(s):

Paula Ossowicz ◽

Proletina Kardaleva ◽

Maya Guncheva ◽

Joanna Klebeko ◽

Ewelina Świątek ◽

...

Keyword(s):

Ionic Liquids ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Binding Constants ◽

Protein Molecule ◽

Binding Mode ◽

Pharmaceutical Ingredients ◽

System A ◽

Static Mechanism

The development of ionic liquids based on active pharmaceutical ingredients (API-ILs) is a possible solution to some of the problems of solid and/or hydrophobic drugs such as low solubility and bioavailability, polymorphism and an alternative route of administration could be suggested as compared to the classical drug. Here, we report for the first time the synthesis and detailed characterization of a series of ILs containing a cation amino acid esters and anion ketoprofen (KETO-ILs). The affinity and the binding mode of the KETO-ILs to bovine serum albumin (BSA) were assessed using fluorescence spectroscopy. All compounds bind in a distance not longer than 6.14 nm to the BSA fluorophores. The estimated binding constants (KA) are in order of 105 L mol−1, which is indicative of strong drug or IL-BSA interactions. With respect to the ketoprofen-BSA system, a stronger affinity of the ILs containing l-LeuOEt, l-ValOBu, and l-ValOEt cation towards BSA is clearly seen. Fourier transformed infrared spectroscopy experiments have shown that all studied compounds induced a rearrangement of the protein molecule upon binding, which is consistent with the suggested static mechanism of BSA fluorescence quenching and formation of complexes between BSA and the drugs. All tested compounds were safe for macrophages.

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Spectroscopic investigation of the interaction of bovine serum albumin with a novel cardiac agent V-09

Spectroscopy An International Journal ◽

10.1155/2008/450257 ◽

2008 ◽

Vol 22 (1) ◽

pp. 43-50 ◽

Cited By ~ 4

Author(s):

Changyun Chen ◽

Meihua Ma ◽

Junqi Zhang ◽

Lichen Wang ◽

Bingren Xiang

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Average Distance ◽

Cardiac Activity ◽

Binding Constants ◽

Entropy Change ◽

Standard Entropy ◽

Förster Energy Transfer ◽

Standard Enthalpy Change

This study employs fluorescence spectroscopy to characterize the binding properties of a newly synthesized cardiac agent, V-09, on bovine serum albumin (BSA). This compound shows the highest cardiac activity in the whole series. The binding constantsKat 25°C and 37°C are obtained, the values are 7.12×104l mol–1, 4.66×104l mol–1, respectively. The standard enthalpy change (ΔH0) and the standard entropy change (ΔS0) are calculated to be –27.13 KJ mol–1and 1.854 J mol–1K–1, which indicated that hydrophobic forces play major role in the interaction between V-09 and BSA. The binding average distance between V-09 and BSA (2.57 nm) is obtained on the basis of the theory of Főrster energy transfer.

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