Fluorescence spectroscopic and molecular docking studies of the binding interaction between the new anaplastic lymphoma kinase inhibitor crizotinib and bovine serum albumin

2017 ◽  
Vol 171 ◽  
pp. 174-182 ◽  
Author(s):  
Ali S. Abdelhameed ◽  
Amer M. Alanazi ◽  
Ahmed H. Bakheit ◽  
Hany W. Darwish ◽  
Hazem A. Ghabbour ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Anaplastic Lymphoma Kinase ◽  
Bovine Serum ◽  
Kinase Inhibitor ◽  
Docking Studies ◽  
Binding Interaction ◽  
Anaplastic Lymphoma Kinase Inhibitor ◽  
Anaplastic Lymphoma

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 Spectroscopic, thermodynamic and molecular docking studies of bovine serum albumin interaction with ascorbyl palmitate food additive

Bioimpacts ◽  
2017 ◽  
Vol 7 (4) ◽  
pp. 241-246 ◽  
Author(s):  
Yousef Sohrabi ◽  
Vahid Panahi-Azar ◽  
Abolfazl Barzegar ◽  
Jafar Ezzati Nazhad Dolatabadi ◽  
Parvin Dehghan
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Ascorbyl Palmitate ◽  
Docking Studies ◽  
Food Additive ◽  
Molecular Docking Studies
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