[Interaction between bovine serum albumin and umbelliferone with/without metal ions of Cu2+ or Zn2+].
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Abstract:
The interaction between bovine serum albumin (BSA) a nd umbelliferone, an active component of Chinese herbs, with or without metal ions was investigated using fluorescence spectroscopy (FS) and UV. The experimental results showed that the umbelliferone molecules inserted into the hydrophobic pockets of BSA and quenched the intrinsic fluorescence of BSA by forming umbelliferone-BSA complex. The mechanism of fluorescence quenching was confirmed combining by both static quenching and nonradiative energy transferring. It was discovered that the apparent association constant (K(A)) increases in the presence of Cu2+ and Zn2+, whereas the spatial-distance (r) between umbelliferone molecule and fluorescent amino acid residues of the BSA and the binding sites (n) of umbelliferone molecules on BSA have no obviously change. Binding of umbelliferone molecules to BSA was a spontaneous supramolecular interaction in which entropy increased and Gibbs free energy decreaed. The interaction of the umbelliferone-BSA was driven mainly by electrostatic force which was enhanced by Cu2+ and Zn2+, thus the contribution of AH to AG increased in the presence of metal ions.Keywords:
Umbelliferone
Bovine serum albumin
Binding constant
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The interaction of quercetin and bovine serum albumin (BSA) was investigated using fluorescence spectroscopy (FS) and ultraviolet spectroscopy (UV). The apparent binding constants (KA) between quercetin and BSA were 2.8 x 10(8) (26 degrees C) and 3.1 x 10(8) (36 degrees C), and the binding sites (n) were 1.7+/-0.02. According to the Forster theory of non-radiation energy transfer, the binding distances (r) were also obtained. The experimental results showed that the quercetin could be inserted into the BSA, quenching the inner fluorescence by forming the quercetin-BSA complex. It was found that both static quenching and non-radiation energy transfer were the main reasons for the fluorescence quenching. The process of binding was a spontaneous molecular interactioln in which entropy increased while Gibbs free energy decreased, indicating that the interaction of quercetin and BSA was driven mainly by hydrophobic force.
Bovine serum albumin
Ultraviolet visible spectroscopy
Binding constant
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Effect of Hydroxyl Substituent on the Interactions between Three Flavonoids and Bovine Serum Albumin
Fluorescence spectroscopy was used to investigate the interactions of bovine serum albumin(BSA) with flavonoids apigenin(Api),genistein(Gen) and galangin(Gal).The fluorescence quenching mechanism of BSA by each compound was studied.The binding constant and binding site number were also measured.The result indicated that BSA was reacted with each compound by hydrophobic force and static quenching mode.The influence of Api,Gen and Gal on the conformation of BSA was investigated using synchronous fluorescence and UV absorption spectroscopy.The interaction strength order of the compounds and BSA was as follows:ApiGalGen,which indicated that the number and site of substituted hydroxyl in each molecule played an important role in the interaction of these compounds with BSA.
Bovine serum albumin
Galangin
Binding constant
Serum Albumin
Hydrophobic effect
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The interaction between nicotinic acid(NTA) and bovine serum albumin(BSA) in physiological solution was investigated by fluorescence spectrometry.The results showed fluorescence intensity of BSA was quenched by NTA based on the dynamic quenching model.The binding constants were obtained by calculation,which were 31.9(293 K) and 72.9 L·mol-1(310 K) respectively.The thermodynamic parameters obtained from measured data showed that the interaction of NTA and BSA was mainly driven by hydrophobic force.Synchronous fluorescence spectrometry and ultraviolet(UV) spectroscopy indicated that NTA did not affect the conformation of BSA.
Bovine serum albumin
Serum Albumin
Fluorescence spectrometry
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Binding constant
Bovine serum albumin
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Bovine serum albumin
Binding constant
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The effects of Cu2+ or Co2+ on the interaction between the rutin and bovine serum albumin(BSA) were investigated by means of UV-Vis and fluorescence spectroscopy.The results show that the fluorescence quenching of BSA by rutin is due to the formation of rutin-BSA complex and quenching mechanism is mainly static quenching.It was discovered that the apparent association constant(KLB) increases in the presence of Cu2+ or Co2+,and the effect of Co2+ is stronger.According to the thermodynamic parameters,the main binding force of rutin and BSA was investigated as hydrophobic interaction,and the presence of metals don't change the type of binding force.
Bovine serum albumin
Binding constant
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The interaction between oleanic acid and bovine serum albumin(BSA)in the presence of metal ions using fluorescence and UV absorption spectrometric methods was studied.Results obtained from analysis of fluorescence spectra indicated that in physiological condition(pH 7.4),the quenching of oleanic acid to BSA is probably a single static quenching process.The binding constant of OA with bovine serum albumin was found to be K=6.16×103 L·mol-1.Whereas,in the presence of Cu2+and Zn2+,the type of BSA intrinsic fluorescence quenching was not changed.It was discovered that the apparent association constant increases in the presence of Cu2+and Zn2+.The number of binding sites of OA on BSA was still about 1.
Bovine serum albumin
Binding constant
Serum Albumin
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The interaction between hesperetin and bovine serum albumin(BSA) was studied in the presence of Cu2 +or Zn2 +by using fluorescence spectroscopy and three-dimensional fluorescence spectrometry.Results indicated that hesperetin could quench the intrinsic fluorescence of BSA,the quenching mechanism was static quenching and the main binding force was Vander Waals force and hydrogen bond.The fluorescence quenching mechanism and the main binding force of BSA did not change in the presence of Cu2 +or Zn2 +.Metal ions could make the peptide chain of BSA into restricted state and hamper the access of hesperetin.Conclusions were made by comparing the quenching constant,binding constant,number of binding sites and quenching efficiency,combined with the changes of three-dimensional fluorescence spectrometry.However,the presence of Cu2 +or Zn2 +may have competition with hesperetin.
Hesperetin
Bovine serum albumin
Binding constant
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Bovine serum albumin
Binding constant
Hydrophobic effect
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Under the imitated physiological conditions (pH = 7.4), the interactions of two novel genistein esterified derivatives, genistein 7-acetylferulic acid ester and genistein 7, 4'-di-acetylferulic acid ester (1 and 2), with bovine serum albumin (BSA) were investigated by the fluorescence and UV-Vis spectroscopy. It was observed that both of them can effectively quench the intrinsic fluorescence of BSA. The results suggested that the fluorescence quenching process of BSA at low concentrations of the compounds may be mainly governed by static quenching mechanisms. The binding constants (KA) and the number of binding sites (n) at different temperatures were calculated. From the thermodynamic parameters, it can be judged that the binding of 1 to BSA involved electrostatic interactions, whereas the binding of 2 to BSA involved hydrogen bonds and Van der Waals forces. The binding average distances r between BSA (donor) and the compounds (acceptor) were determined to be 2.63 nm and 2.92 nm respectively based on the Forster theory. Besides, the interactions of BSA with the compounds did not change the conformation of BSA and the binding of compounds to BSA is near tryptophan subunit via synchronous fluorescence spectrometry.
Bovine serum albumin
Acceptor
Hydrophobic effect
Binding constant
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