Plasma Protein Binding of Anisomelic Acid: Spectroscopy and Molecular Dynamic Simulations

Anisomelic acid (AA) is a macrocyclic cembranolide compound extracted from Anisomeles herbal species. Recently, we have shown that AA possesses both anticancer and antiviral activity. However, to date, the plasma protein binding properties of AA are unknown. Here, we describe the molecular interacti...

Full description

Saved in:
Bibliographic Details
Published in:Journal of chemical information and modeling 2016-12, Vol.56 (12), p.2401-2412
Main Authors: Senthilkumar, Rajendran, Marimuthu, Parthiban, Paul, Preethy, Manojkumar, Yesaiyan, Arunachalam, Sankaralingam, Eriksson, John E, Johnson, Mark S
Format: Article
Language:English
Subjects:
Acids
Animals
Binding sites
Cattle
Diterpenes - metabolism
Humans
Hydrophobic and Hydrophilic Interactions
Molecular Docking Simulation
Molecular Dynamics Simulation
Molecules
Plasma
Protein Binding
Proteins
Serum Albumin - metabolism
Serum Albumin, Bovine - metabolism
Simulation
Spectrum analysis
Thermodynamics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Anisomelic acid (AA) is a macrocyclic cembranolide compound extracted from Anisomeles herbal species. Recently, we have shown that AA possesses both anticancer and antiviral activity. However, to date, the plasma protein binding properties of AA are unknown. Here, we describe the molecular interactions of AA with two serum proteins, human serum albumin (HSA) and bovine serum albumin (BSA), adopting multiple physicochemical methods. Besides, molecular docking and dynamics simulations were performed to predict the interaction mode and the dynamic behavior of AA with HSA and BSA. The experimental results revealed that hydrophobic forces play a significant part in the interaction of AA to HSA and BSA. The outcomes of the principal components analysis (PCA) of the poses based on root-mean-squared distances showed less variation in AA–HSA, opposed to what is seen for BSA–AA. Furthermore, binding free energies estimated for AA–HSA and AA–BSA complexes at different temperatures (298, 303, 308, and 313 K) based on molecular mechanics-generalized Born surface area (MMGBSA) approaches were well correlated with our experimental results.
ISSN:1549-9596
1549-960X
DOI:10.1021/acs.jcim.6b00445