Exploration of the binding between cuminol and bovine serum albumin through spectroscopic, molecular docking and molecular dynamics methods

2021 ◽  
pp. 1-9
Author(s):  
Mohd Sajid Ali ◽  
Md Tabish Rehman ◽  
Hamad A. Al-Lohedan ◽  
Mohamed Fahad AlAjmi
Keyword(s):  
Molecular Dynamics ◽  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Molecular Dynamics Methods

scholarly journals Aggregation behavior of cetyldimethylethylammonium bromide under the influence of bovine serum albumin in aqueous/electrolyte solutions at various temperatures and compositions: conductivity and molecular dynamics study

RSC Advances ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 6556-6567 ◽  
Author(s):  
Md. Farid Ahmed ◽  
Mohammad Robel Molla ◽  
Mousumi Saha ◽  
Imrul Shahriar ◽  
Mohammad Saidur Rahman ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Aqueous Electrolyte ◽  
Electrolyte Solutions ◽  
Aggregation Behavior ◽  
Aqueous Electrolyte Solutions ◽  
Molecular Dynamics Methods

Herein, we have investigated the interaction of bovine serum albumin with a cetyldimethylethylammonium bromide,viaa conductivity and molecular dynamics methods in the absence/presence of electrolyte solutions.

A spectroscopic and molecular dynamics simulation approach towards the stabilizing effect of ammonium-based ionic liquids on bovine serum albumin

2017 ◽  
Vol 41 (19) ◽  
pp. 10712-10722 ◽  
Author(s):  
Lakkoji Satish ◽  
Sabera Millan ◽  
Krishnendu Bera ◽  
Sujata Mohapatra ◽  
Harekrushna Sahoo
Keyword(s):  
Molecular Dynamics ◽  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Dynamics Simulation ◽  
Thermal Unfolding ◽  
Simulation Approach ◽  
Stabilizing Effect ◽  
Theoretical Evidence

Experimental and theoretical evidence in support of the stabilizing effect of ammonium-based ionic liquids on thermal unfolding/refolding of bovine serum albumin is provided in this article.

scholarly journals Study of Interaction Between Bovine Serum Albumin and Dolutegravir Intermediate: Fluorescence and Molecular Docking Analysis

2021 ◽  
Vol 11 (5) ◽  
pp. 13102-13110
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Pocket ◽  
Docking Analysis ◽  
Free Binding Energy ◽  
Steady State Fluorescence Spectroscopy ◽  
Incremental Addition ◽  
Molecular Docking Analysis

Novel (4R,12aS)-7-methoxy-4-methyl-6,8-dioxo-3,4,6,8,12,12a-hexahydro-2H-pyrido-[1',2':-4,5]-pyrazino[2,1-b][1,3]oxazine-9-carboxylic acid (L) was synthesized and characterised. The interaction between bovine serum albumin (BSA) with L was scrutinized by steady-state fluorescence spectroscopy, fluorescence anisotropy, fluorescence lifetime, and molecular docking methods. The fluorescence titration experiments of BSA resulted in fluorescence quenching with the incremental addition of L. The conformational binding of L to BSA has been investigated by molecular docking analysis. The molecular probe's best conformation showed the affinity as free binding energy release of -7.93 Kcal/mol. The docking analysis confirms that ligand binds in the near vicinity of TRP-213 in the binding pocket of subdomain IIA.

Sign in / Sign up

Export Citation Format

Share Document