Destabilization of Human Serum Albumin by Ionic Liquids Studied Using Enhanced Molecular Dynamics Simulations

2016 ◽  
Vol 120 (47) ◽  
pp. 12079-12087 ◽  
Author(s):  
Vance W. Jaeger ◽  
Jim Pfaendtner
Keyword(s):  
Molecular Dynamics ◽  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Dynamics Simulations ◽  
Dynamics Simulations

Interactions between the antiviral drug telaprevir and human serum albumin: a combined study with spectroscopic methods and molecular modeling

2018 ◽  
Vol 42 (12) ◽  
pp. 9791-9800 ◽  
Author(s):  
Xinnuo Xiong ◽  
Ruixue Gan ◽  
Zili Suo ◽  
Peixiao Tang ◽  
Shuangshuang Zhang ◽  
...  
Keyword(s):  
Molecular Dynamics ◽  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Dynamics Simulations ◽  
Antiviral Drug ◽  
Spectroscopic Methods ◽  
Binding Mechanism ◽  
Dynamics Simulations

The binding mechanism between telaprevir and human serum albumin was explored by combining spectroscopic methods and molecular dynamics simulations.

scholarly journals A Molecular Dynamics Approach to Ligand-Receptor Interaction in the Aspirin-Human Serum Albumin Complex

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
H. Ariel Alvarez ◽  
Andrés N. McCarthy ◽  
J. Raúl Grigera
Keyword(s):  
Molecular Dynamics ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Energy Difference ◽  
Receptor Interaction ◽  
Affinity Constant ◽  
External Work ◽  
Dynamics Simulations ◽  
Work Done

In this work, we present a study of the interaction between human serum albumin (HSA) and acetylsalicylic acid (ASA, C9H8O4) by molecular dynamics simulations (MD). Starting from an experimentally resolved structure of the complex, we performed the extraction of the ligand by means of the application of an external force. After stabilization of the system, we quantified the force used to remove the ASA from its specific site of binding to HSA and calculated the mechanical nonequilibrium external work done during this process. We obtain a reasonable value for the upper boundary of the Gibbs free energy difference (an equilibrium thermodynamic potential) between the complexed and noncomplexed states. To achieve this goal, we used the finite sampling estimator of the average work, calculated from the Jarzynski Equality. To evaluate the effect of the solvent, we calculated the so-called “viscous work,” that is, the work done to move the aspirin in the same trajectory through the solvent in absence of the protein, so as to assess the relevance of its contribution to the total work. The results are in good agreement with the available experimental data for the albumin affinity constant for aspirin, obtained through quenching fluorescence methods.

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