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

Senthil Rajendran, Parthiban Marimuthu, Preethy Paul, Yesaiyan Manojkumar, Sankaralingam Arunachalam, John Eriksson, Mark S Johnson

Research output: Contribution to journalArticleScientificpeer-review

25 Citations (Scopus)


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.
Original languageUndefined/Unknown
Pages (from-to)2401–2412
JournalJournal of Chemical Information and Modeling
Issue number12
Publication statusPublished - 2016
MoE publication typeA1 Journal article-refereed

Cite this