Static and Dynamic Aspects of Supramolecular Interactions of Coumarin 153 and Fluorescein with Bovine Serum Albumin

The static and dynamic aspects of supramolecular interactions between coumarin 153 (C153) and fluorescein (FL) with bovine serum albumin (BSA) has been studied by spectroscopic techniques. Both dyes were found to form 1 : 1 complexes with BSA, with binding constants 2.9 ± 0.3 × 105 M–1 and 2.1 ± 0.2 × 105 M–1 for C153 and FL respectively. The binding site of C153 has been determined by steady-state fluorescence resonance energy transfer, site marker competitive experiments, and a molecular docking study. Our studies indicate that C153 binds to domain IIIA of BSA whereas FL binds non-specifically. Denaturation characteristics of the C153 and FL binding region of BSA were found to be very different to global denaturation. Furthermore, kinetics of binding has been studied by the stopped-flow method. The observed rate constants were found to be 8.8 s–1 and 5.9 s–1 for C153 and FL respectively.

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Exploring the thermodynamics and conformational aspects of nicotinic acid binding with bovine serum albumin: a detailed calorimetric, spectroscopic and molecular docking study

RSC Advances ◽

10.1039/c5ra28028a ◽

2016 ◽

Vol 6 (41) ◽

pp. 34754-34769 ◽

Cited By ~ 17

Author(s):

Tarlok Singh Banipal ◽

Amandeep Kaur ◽

Imran Ahmd Khan ◽

Parampaul Kaur Banipal

Keyword(s):

Molecular Docking ◽

Light Scattering ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Docking Study ◽

Vitamin B ◽

Spectroscopic Techniques ◽

Molecular Docking Study ◽

Binding Interaction

An attempt to obtain a physicochemical and conformational outlook on the binding interaction of vitamin B3 (NA) with a model transport protein BSA using calorimetry, light scattering, molecular docking, and spectroscopic techniques.

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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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Molecular interaction of cationic gemini surfactant with bovine serum albumin: A spectroscopic and molecular docking study

Process Biochemistry ◽

10.1016/j.procbio.2014.01.020 ◽

2014 ◽

Vol 49 (4) ◽

pp. 623-630 ◽

Cited By ~ 50

Author(s):

Muzaffar Ul Hassan Mir ◽

Jitendra Kumar Maurya ◽

Shahnawaz Ali ◽

Shah Ubaid-ullah ◽

Abbul Bashar Khan ◽

...

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Molecular Interaction ◽

Bovine Serum ◽

Gemini Surfactant ◽

Docking Study ◽

Molecular Docking Study ◽

Cationic Gemini Surfactant

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Spectroscopic and molecular docking study to understand the binding interaction of rosiglitazone with bovine serum albumin in presence of valsartan

Journal of Luminescence ◽

10.1016/j.jlumin.2018.01.017 ◽

2018 ◽

Vol 197 ◽

pp. 200-210 ◽

Cited By ~ 3

Author(s):

Satish Pawar ◽

Rakesh Joshi ◽

Divya Ottoor

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Docking Study ◽

Molecular Docking Study ◽

Binding Interaction

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Spectroscopic and molecular docking study on the structure-affinity relationship and mechanism in the interaction of genistein and its derivatives with bovine serum albumin

Luminescence ◽

10.1002/bio.3333 ◽

2017 ◽

Vol 32 (8) ◽

pp. 1368-1384 ◽

Cited By ~ 4

Author(s):

Yu Guo ◽

Lixian Shen ◽

Xu Yao ◽

Yang Liu ◽

Yunmei Liu ◽

...

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Docking Study ◽

Molecular Docking Study

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Evaluation of Biophysical Interaction between Newly Synthesized Pyrazoline Pyridazine Derivative and Bovine Serum Albumin by Spectroscopic and Molecular Docking Studies

Journal of Spectroscopy ◽

10.1155/2019/3848670 ◽

2019 ◽

Vol 2019 ◽

pp. 1-12 ◽

Cited By ~ 6

Author(s):

Abdulrahman A. Al-Mehizia ◽

Ahmed H. Bakheit ◽

Seema Zargar ◽

Mashooq A. Bhat ◽

Majid Mohammed Asmari ◽

...

Keyword(s):

Molecular Docking ◽

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Resonance Energy Transfer ◽

Resonance Energy ◽

Docking Studies ◽

Investigational Drug ◽

Spectroscopic Techniques ◽

Binding Interaction

In this research, the pyrazoline pyridazine derivative 7-methyl-2-phenyl-4-(3,4,5-trimethoxyphenyl)-2H-pyrazolo[3,4-d]pyridazine (5d) was studied for its interaction with bovine serum albumin (BSA). Various spectroscopic techniques along with molecular docking analysis were utilized to understand the mechanism of interaction. The quenching of BSA fluorescence by using investigational drug 5d was the basic principle for the methodology. Spectrofluorometric methods and UV-absorption studies were conducted for exploration of the 5d and BSA binding mechanism. The fluorescence quenching mechanism involved in BSA and 5d interaction was static quenching, and a complex formation also occurred between them. Both enthalpy and entropy attained positive values suggesting involvement of hydrophobic forces in BSA and 5d interaction. The Förster distance of 2.23 nm was calculated by fluorescence resonance energy transfer (FRET). An alteration in BSA secondary structure was proven from the conformational studies of BSA-5d interaction. This binding interaction study provided a basis to comprehend the binding interaction between 5d and BSA. These results provided information about sites of BSA involved in its interaction with 5d.

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