Binding assessment of two arachidonic-based synthetic derivatives of adrenalin with β-lactoglobulin: Molecular modeling and chemometrics approach

Gholami, S ; Sharif University of Technology | 2015

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  1. Type of Document: Article
  2. DOI: 10.1016/j.bpc.2015.10.001
  3. Publisher: Elsevier , 2015
  4. Abstract:
  5. A computational approach to predict the main binding modes of two adrenalin derivatives, arachidonoyl adrenalin (AA-AD) and arachidonoyl noradrenalin (AA-NOR) with the β-lactoglubuline (BLG) as a nano-milk protein carrier is presented and assessed by comparison to the UV-Vis absorption spectroscopic data using chemometric analysis. Analysis of the spectral data matrices by using the multivariate curve resolution-alternating least squares (MCR-ALS) algorithm led to the pure concentration calculation and spectral profiles resolution of the chemical constituents and the apparent equilibrium constants computation. The negative values of entropy and enthalpy changes for both compound indicated the essential role of hydrogen bonding and van der Waals interactions as main driving forces in stabilizing protein-ligand complex. Computational studies predicted that both derivatives are situated in the calyx pose and remained in that pose during the whole time of simulation with no any significant protein structural changes which pointed that the BLG could be considered as a suitable carrier for these catecholamine compounds
  6. Keywords:
  7. Arachidonoyl adrenalin ; Arachidonoyl noradrenalin ; Binding modes ; Chemometrics ; Molecular docking ; Molecular dynamics simulation ; Beta lactoglobulin ; Catecholamine ; Milk protein ; Noradrenalin ; Structural protein ; Unclassified drug ; Absorption ; Algorithm ; Chemical composition ; Chemometric analysis ; Complex formation ; Conformational transition ; Crystal structure ; Enthalpy ; Entropy ; Equilibrium constant ; Hydrogen bond ; Ligand binding ; Molecular dynamics ; Molecular model ; Priority journal ; Protein binding ; Protein conformation ; Quantum chemistry ; Spectroscopy ; Thermodynamics
  8. Source: Biophysical Chemistry ; Volume 207 , 2015 , Pages 97-106 ; 03014622 (ISSN)
  9. URL: http://www.sciencedirect.com/science/article/pii/S0301462215300569