scholarly journals Binding studies of paeonolum with bovine serum albumin using spectroscopic methods

2007 ◽  
Vol 21 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Chang-yun Chen ◽  
Xiao-tian Gu ◽  
Jia-hong Zhou
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Interaction Process ◽  
Spectroscopic Methods ◽  
Spectroscopic Techniques ◽  
Bioactive Components ◽  
Binding Studies ◽  
Binding Interaction ◽  
Physiological Conditions

Fluorescence and UV spectroscopic techniques were used to investigate the interaction of Paeonolum, one of the major bioactive components isolated from the bark of peony plant, with bovine serum albumin (BSA). Results obtained reveal that a binding interaction occurs between paeonolum and BSA under physiological conditions, and the interaction can quench the fluorescence of BSA originating from the complex formation between paeonolum and BSA. In addition, according to the thermodynamics parameters of this interaction process, it appears that this binding interaction is mainly hydrophobic in nature.

Studies on the Interaction between Imidacloprid and Bovine Serum Albumin by Spectrometry

2013 ◽  
Vol 726-731 ◽  
pp. 199-203
Author(s):  
Rui Xin Guo ◽  
Zhi Liang Wang ◽  
Zhi Jun Hu ◽  
Guo Ling Li ◽  
Jian Qiu Chen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Fluorescence Spectrum ◽  
Bovine Serum ◽  
Synchronous Fluorescence ◽  
Binding Studies ◽  
Single Class ◽  
Physiological Conditions ◽  
Synchronous Fluorescence Spectrometry ◽  
Hoff Equation

The binding studies of imidacloprid to bovine serum albumin (BSA) were investigated by UV-Vis absorption spectrum, fluorescence spectrum and synchronous fluorescence spectrometry. Under the simulative physiological conditions, fluorescence data revealed the presence of a single class of binding site on BSA and the dynamic quenching constants () were 6.851×104 L.mol-1 and 5.813×104 L.mol-1 at 310 and 315 K, respectively, proving the mode of action of imidacloprid with BSA as a static quenching. In addition, according to the Vant Hoff equation, ΔGθ <0 showed="" the="" combination="" of="" imidacloprid="" and="" bsa="" was="" a="" spontaneous="" process="" h="" sup="">θ <0 and="" s="" sup="">θ> 0, indicated an electrostatic interaction process. At the same time, synchronous fluorescence spectrum of BSA could tell us whether the conformation of BSA was changed by imidacloprid.

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

2019 ◽  
Vol 2019 ◽  
pp. 1-12 ◽  
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.

scholarly journals Interaction of Conazole Pesticides Epoxiconazole and Prothioconazole with Human and Bovine Serum Albumin Studied Using Spectroscopic Methods and Molecular Modeling

2021 ◽  
Vol 22 (4) ◽  
pp. 1925
Author(s):  
Katarína Golianová ◽  
Samuel Havadej ◽  
Valéria Verebová ◽  
Jozef Uličný ◽  
Beáta Holečková ◽  
...  
Keyword(s):  
Molecular Modeling ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Three Dimensional ◽  
Association Constants ◽  
Van Der Waals Interactions ◽  
Spectroscopic Methods ◽  
Spectroscopic Techniques ◽  
Conformation Changes

The interactions of epoxiconazole and prothioconazole with human serum albumin and bovine serum albumin were investigated using spectroscopic methods complemented with molecular modeling. Spectroscopic techniques showed the formation of pesticide/serum albumin complexes with the static type as the dominant mechanism. The association constants ranged from 3.80 × 104–6.45 × 105 L/mol depending on the pesticide molecule (epoxiconazole, prothioconazole) and albumin type (human or bovine serum albumin). The calculated thermodynamic parameters revealed that the binding of pesticides into serum albumin macromolecules mainly depended on hydrogen bonds and van der Waals interactions. Synchronous fluorescence spectroscopy and the competitive experiments method showed that pesticides bind to subdomain IIA, near tryptophan; in the case of bovine serum albumin also on the macromolecule surface. Concerning prothioconazole, we observed the existence of an additional binding site at the junction of domains I and III of serum albumin macromolecules. These observations were corroborated well by molecular modeling predictions. The conformation changes in secondary structure were characterized by circular dichroism, three-dimensional fluorescence, and UV/VIS absorption methods.

scholarly journals Characterizing the binding interaction of astilbin with bovine serum albumin: a spectroscopic study in combination with molecular docking technology

RSC Advances ◽  
2018 ◽  
Vol 8 (13) ◽  
pp. 7280-7286 ◽  
Author(s):  
Jianli Liu ◽  
Yonglin He ◽  
Dan Liu ◽  
Yin He ◽  
Zhipeng Tang ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Spectroscopic Study ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Binding Interaction

The interaction of astilbin with bovine serum albumin was confirmed by multi-spectroscopic techniques and molecular docking methods.

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

RSC Advances ◽  
2016 ◽  
Vol 6 (41) ◽  
pp. 34754-34769 ◽  
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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