title: Plasma Protein Binding of Anisomelic Acid: Spectroscopy and Molecular Dynamic Simulations.
abstract: 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.
authors.affiliation: Faculty of Science and Engineering, Cell Biology, Åbo Akademi University , Tykistökatu 6A, FI-20520 Turku, Finland.
authors.forename: Rajendran
authors.identifier: 0000-0002-8705-150X
authors.initials: R
authors.lastname: Senthilkumar
authors.affiliation: Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University , Tykistökatu 6A, FI-20520 Turku, Finland.
authors.forename: Parthiban
authors.initials: P
authors.lastname: Marimuthu
authors.affiliation: Faculty of Science and Engineering, Cell Biology, Åbo Akademi University , Tykistökatu 6A, FI-20520 Turku, Finland.
authors.forename: Preethy
authors.initials: P
authors.lastname: Paul
authors.affiliation: School of Chemistry, Bharathidasan University , Tiruchirappalli-620 024, Tamil Nadu, India.
authors.forename: Yesaiyan
authors.initials: Y
authors.lastname: Manojkumar
authors.affiliation: School of Chemistry, Bharathidasan University , Tiruchirappalli-620 024, Tamil Nadu, India.
authors.forename: Sankaralingam
authors.identifier: 0000-0003-0813-1032
authors.initials: S
authors.lastname: Arunachalam
authors.affiliation: Faculty of Science and Engineering, Cell Biology, Åbo Akademi University , Tykistökatu 6A, FI-20520 Turku, Finland.
authors.forename: John E
authors.initials: JE
authors.lastname: Eriksson
authors.affiliation: Structural Bioinformatics Laboratory, Biochemistry, Faculty of Science and Engineering, Åbo Akademi University , Tykistökatu 6A, FI-20520 Turku, Finland.
authors.forename: Mark S
authors.initials: MS
authors.lastname: Johnson
mesh_terms: D000818:Animals; D002417:Cattle; D004224:Diterpenes / Q000378:metabolism*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D012709:Serum Albumin / Q000378:metabolism*; D012710:Serum Albumin, Bovine / Q000378:metabolism*; D013816:Thermodynamics
chemical_list: D004224:Diterpenes; D012709:Serum Albumin; C000613048:anisomelic acid; D012710:Serum Albumin, Bovine