Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin

Wang, Yanqing; Zhang, Hongmei; Zhang, Gencheng; Wei, Tao; Fei, Zhenghao; Liu, Zongtang

doi:10.1016/j.jpba.2007.01.001

Cited by 171 publications

(64 citation statements)

References 39 publications

(52 reference statements)

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“…These above observations signify that with the addition of SM and SMT, the peptide strands of BSA molecules were extended more and hydrophobicity was decreased [32] and this perspective was also validated by the following fluorescence spectroscopy studies and its quenching mechanism. Table 1, Figs.…”

Section: Absorption Spectroscopic Studiessupporting

confidence: 59%

Binding of Sulfamerazine and Sulfamethazine to Bovine Serum Albumin and Nitrogen Purine Base Adenine: A Comparative Study

Rajendiran

Thulasidhasan

2015

ILCPA

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ABSTRACT. Quenching of bovine serum albumin (BSA) and DNA base (adenine) by sulfamerazine (SM) and sulfamethazine (SMT) was studied using UV-visible, fluorescence cyclic voltammetry and molecular docking methods. A strong fluorescence quenching reaction of SM and SMT to BSA/adenine was observed and the quenching mechanism was suggested as static. Both drugs can bind to BSA and adenine with stoichiometric ratio of 1:1 and the protein -drug complexes are stabilized mainly by hydrogen bonds and van der Waals interaction. Compared to SM, SMT contributes substantially higher binding efficiency with BSA/adenine. With addition of drug solution to the adenine/BSA, the oxidation and the reduction peaks shifted towards high and low potentials, respectively. R o , J, r and E values in the BSA-drugs are higher than that of adeninedrug molecules suggest that binding of the sulfa drugs with BSA is higher than adenine -drug molecules. Docking method specify that bioactive site of sulfa drugs moiety, the aniline group is interacted with the BSA molecules.

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Section: Absorption Spectroscopic Studiessupporting

confidence: 59%

Binding of Sulfamerazine and Sulfamethazine to Bovine Serum Albumin and Nitrogen Purine Base Adenine: A Comparative Study

Rajendiran

Thulasidhasan

2015

ILCPA

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Section: Fluorescence Spectroscopic Investigation Of the Binding Mechmentioning

confidence: 99%

“…The addition of compound 3 caused the BSA fluorescence intensity to be quenched in a concentration dependent way (Figure 3), with no BSA peak shift or shape alteration. The experimental quenching effect can be either classified as a dynamic or a static type of quenching [22,39]. Based on their temperature dependence, the two types of quenching can be further identified, i.e., higher temperatures yield higher quenching constants in dynamic quenching, while the opposite is always true in the case of static quenching.…”

Section: Fluorescence Spectroscopic Investigation Of the Binding Mechmentioning

confidence: 99%

“…A model protein that is frequently used to represent this albumins family in experimental studies is the bovine serum albumin (BSA) [19,20]. BSA is a structural homologue to the human serum albumin (HSA) with a well-studied structure [21][22][23][24][25]. Numerous studies have been published reporting BSA-drug binding interactions using spectroscopic tools [18,20,26,27].…”

Section: Introductionmentioning

confidence: 99%

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Synthesis and Biophysical Insights into the Binding of a Potent Anti-Proliferative Non-symmetric Bis-isatin Derivative with Bovine Serum Albumin: Spectroscopic and Molecular Docking Approaches

et al. 2017

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As part of the research endeavors to combat cancer, a non-symmetric bis-isatin derivative (compound 3) was synthesized and showed a significant anti-proliferative potency. The current study provides a comprehensive characterization of the interaction of compound 3 with the drug-transporting protein bovine serum albumin (BSA) via the use of spectroscopic tools along with molecular docking studies. Fluorescence spectral measurements showed that the BSA intrinsic fluorescence can be significantly quenched by the addition of compound 3 and the formation of a non-fluorescent complex. Further measurements revealed a static type of quenching with Stern-Volmer and Linweaver-Burk constants of 10 5 . The thermodynamic parameters of the binding were calculated to be ∆S • 105.09 ± 5.32 with ∆H • of −0.72 ± 0.71 and negative ∆G • values. In addition, synchronous fluorescence and 3D fluorescence spectroscopy suggested that compound 3 did not induce conformational changes in BSA. Site competition experiments revealed that compound 3 competes with warfarin within the BSA binding domain (Sudlow site I). This was further confirmed by the molecular docking results showing a binding energy of −25.93 kJ/mol for compound 3-BSA. Hence, the observed results in the present study assumed that the compound 3-BSA binding is spontaneous, involving electrostatic forces and hydrogen bonding.

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“…This phenomenon of upward curvature also reported in many observations, done with many ligands and proteomics observation [27][28][29]. Modified Stern-Volmer equation [27] can be applied to resolve such situation, where both static and dynamic quenching are operative, in view of exponential form of the model of the sphere of action, V, equation (2) [30][31][32] or on the basis of quadratic dependence [33][34][35] upon quencher concentration model: from equation 2.…”

Section: Citationmentioning

confidence: 62%

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

Rabbi¹,

Didaruzzaman²,

Sultan³

2015

J Bioanal Biomed

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Citation: Rabbi SNI, Sultan MdZ, Sohel MdD, Sultan MdZ (2015) Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy. J Bioanal Biomed 7: 164-170. doi:10.4172/1948-593X.1000138 Copyright: © 2015 Rabbi SNI, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. AbstractThe interaction of an anti-gout drug, febuxostat was studied with bovine serum albumin (BSA) applying fluorescence quenching method for the first time. Interaction parameter and magnitude of the force indicated for both, dynamic and static quenching in between febuxostat and BSA protein. Thermodynamic studies indicated for both hydrogen and hydrophobic interactions, observed at 280 nm and only hydrophobic at 293 nm excitation wavelength. Negative ΔH o and positive ΔS o , indicated for distinctive characteristics for the existence of both, hydrogen and hydrophobic binding throughout the interactions. The binding constant K b at λ ex =280 nm was 3.467 × 10 3 µM -1 and 4.943 × 10 3 µM -1 at 298 and 308 K temperature whereas, 5.54 × 10 3 µM -1 and 4.44 × 10 3 µM -1 was noted during excitation at λ ex =293 nm wavelength. The K b values in different temperatures assumed that the stability of binding increased with the increase of temperature at λ ex =280 nm, but reverse effect was experienced at an excitation wavelength of λ ex =293 nm. The number of bound febuxostat molecules per BSA protein was found ~1.5 at both 298 and 308 K. Study of Interaction between

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Spectroscopic studies on the interaction between silicotungstic acid and bovine serum albumin

Cited by 171 publications

References 39 publications

Binding of Sulfamerazine and Sulfamethazine to Bovine Serum Albumin and Nitrogen Purine Base Adenine: A Comparative Study

Binding of Sulfamerazine and Sulfamethazine to Bovine Serum Albumin and Nitrogen Purine Base Adenine: A Comparative Study

Synthesis and Biophysical Insights into the Binding of a Potent Anti-Proliferative Non-symmetric Bis-isatin Derivative with Bovine Serum Albumin: Spectroscopic and Molecular Docking Approaches

Study of Interaction between Febuxostat and Bovine Serum Albumin by Fluorescence Spectroscopy

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