title: Spectroscopic and dynamic properties of arachidonoyl serotonin- β-lactoglobulin complex: A molecular modeling and chemometric study.
abstract: UV-Vis absorption data of β-lactoglobulin (BLG) and arachidonoyl serotonin (AA-5HT) in BLG complex were examined and analyzed using chemometrics method. Analysis of the spectral data matrices by using the multivariate curve resolution-alternating least squares (MCR-ALS) algorithm resulted to the pure concentration calculation and spectral profiles resolution of the chemical constituents and the values of (6.433±0.019)×10(4)M(-1), (4.532±0.007)×10(4)M(-1), (3.364±0.010)×10(4)M(-1) and (2.977±0.013)×10(4)M(-1) as estimated equilibrium constants at 288, 293, 298 and 303K, respectively. The number of chemical constituents involved in the interaction which was extracted by PCA method were free and bound BLG. The spontaneity of the binding process and critical role of hydrogen bonding and van der Waals interactions in stabilizing protein-ligand complex have been designated by negative values of Gibbs free energy, entropy and enthalpy changes. Molecular docking study showed that AA-5HT binds to Val(41), Leu(39), Leu(54), Ile(71), Phe(82), Asn(90), Val(92), Phe(105), Met(107), Glu(108) with the free binding energy of -37.478kJ/mol. Computational studies predicted that in spite of serotonin (5HT) which anchors to the outer surface of BLG by hydrogen bonds, AA-5HT is situated in the calyx pose and stayed there during the entire time of simulation. This binding is accompanying with no apparent influence on secondary structure and partially destabilization of tertiary structure of BLG which pointed the suitability of this protein as drug carrier for AA-5HT.
authors.affiliation: Department of Chemistry, University of Isfahan, Isfahan 81746-73441, Iran.
authors.forename: Samira
authors.initials: S
authors.lastname: Gholami
authors.affiliation: Department of Chemistry, University of Isfahan, Isfahan 81746-73441, Iran. Electronic address: bordbar@chem.ui.ac.ir.
authors.forename: Abdol-Khalegh
authors.initials: AK
authors.lastname: Bordbar
authors.affiliation: Department of Chemistry, University of Isfahan, Isfahan 81746-73441, Iran.
authors.forename: Nadia
authors.initials: N
authors.lastname: Akvan
mesh_terms: D001095:Arachidonic Acids / Q000378:metabolism*; D006860:Hydrogen Bonding; D048088:Informatics; D007782:Lactoglobulins / Q000737:chemistry* / Q000378:metabolism*; D008024:Ligands; D062105:Molecular Docking Simulation; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D017433:Protein Structure, Secondary; D012399:Rotation; D012701:Serotonin / Q000031:analogs & derivatives* / Q000378:metabolism; D013057:Spectrum Analysis; D013816:Thermodynamics
chemical_list: D001095:Arachidonic Acids; D007782:Lactoglobulins; D008024:Ligands; C114007:arachidonoylserotonin; D012701:Serotonin
keywords: Arachidonoyl serotonin (AA-5HT); Binding modes; Molecular docking; Molecular dynamics simulation; Multivariate curve resolution–alternating least squares (MCR–ALS); UV–Vis absorption