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

: Senthilkumar R, Marimuthu P, Paul P, Manojkumar Y, Arunachalam S, Eriksson JE, Johnson MS

Publisher: AMER CHEMICAL SOC

: 2016

: Journal of Chemical Information and Modeling

: JOURNAL OF CHEMICAL INFORMATION AND MODELING

: J CHEM INF MODEL

: 56

: 12

: 2401

: 2412

: 12

: 1549-9596

DOI: https://doi.org/10.1021/acs.jcim.6b00445

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 RSA 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-generalised Born surface area (MMGBSA) approaches were well correlated with our experimental results.