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.

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.

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.

Interaction between carisoprodol and bovine serum albumin and effect of β-cyclodextrin on binding: insights from molecular docking and spectroscopic techniques

RSC Advances ◽  
2016 ◽  
Vol 6 (68) ◽  
pp. 63463-63471 ◽  
Author(s):  
Mallavva B. Bolattin ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Sheshagiri R. Dixit ◽  
Shivamurti A. Chimatadar
Keyword(s):  
Amino Acids ◽  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Techniques ◽  
Hydrophobic Amino Acids

Interactions between the BSA and CAP in the docked model. Figure showing H-bonding interactions and carisoprodol surrounded by hydrophobic amino acids Leu249, Leu250 and Gly247 in subdomain IIA.

Synthesis, Molecular Docking, BSA, and in-vitro reactivation study of imidazopyridine oxime against paraoxon inhibited acetylcholinesterase

2021 ◽  
Vol 17 ◽  
Author(s):  
Ashima Thakur ◽  
Jayant Patwa ◽  
Abha Sharma ◽  
Swaran Jeet Flora
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
In Silico ◽  
Bovine Serum ◽  
Enzymatic Assay ◽  
Acid Dissociation ◽  
Acid Dissociation Constant ◽  
Spectroscopic Techniques

Aim: To synthesize and evaluate the fused heterocyclic imidazopyridine oxime as a reactivator against paraoxon inhibited acetylcholinesterase. Background: Organophosphorus compounds (OPs) include parathion, malathion, chlorpyrifos, monocrotophos, and diazinon which are commonly used in agriculture for enhancing agricultural productivity via killing crop-damaging pests. However, people may get exposed to OPs pesticides unintentionally/intentionally via ingestion, inhalation or dermal. The current treatment regimen includes reactivator such as mono or bis-pyridinium oximes along with anticholinergic and an anticonvulsant drugs are recommended for the treatment of OP poisoning. Unfortunately, the drawback of the existing reactivator is that owing to the permanent charge present on the pyridinium makes them inefficient to cross the blood-brain barrier (BBB) and reactivate OP-inhibited central nervous system (CNS) acetylcholinesterase. Therefore, there is a need of reactivator that could cross the BBB and reactivate the OP inhibited acetylcholinesterase. Objective: The objectives of the study were synthesis, molecular docking, BSA binding and in-vitro estimation of oximes of various substituted imidazo [1,2-a]pyridine against paraoxon inhibited acetylcholinesterase. Method: The reactivators were synthesized in three steps and characterized using various spectroscopic techniques. Molecular docking study was performed on 2WHP and 3ZLV PDB using Autodock tool. The acid dissociation constant (pKa) of oximes was calculated experimentally and drug-likeness properties of the oximes were calculated In silico using mole inspiration and Swiss ADME software. The binding of oximes with bovine serum albumin (BSA) was also investigated by UV-Vis spectrophotometer. The reactivation potential of the oximes was determined by in vitro enzymatic assay. Result: in-silico study inferred that synthesized molecules fulfilled the parameters that required for a successful CNS drug candidate. Further, in-vitro enzymatic assay indicated reasonable reactivation potential of the oximes against paraoxon-inhibited AChE. The binding of oximes with bovine serum albumin (BSA) revealed static quenching of intrinsic fluorescence of BSA by oxime. The binding constant value and number of binding sites were found 0.24 mol-1 and 1 respectively. Conclusion: The results of study concluded that this scaffold could be used for further designing of more efficient uncharged reactivators.

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