Atomistic Simulations for Investigating Structural Stability and Selecting Initial Adsorption Orientation of Lysozyme and Apo-α-Lactalbumin at Hydrophobic and Hydrophilic Surfaces

  • Author / Creator
    Pansri, Siriporn
  • Molecular dynamics (MD) simulations were performed to investigate the structural stability of lysozyme and apo-α-lactalbumin under physiological pH and solution. Upon introduction to the solution, apo-α-lactalbumin showed lower stability than lysozyme with higher backbone root mean square fluctuation (RMSF) of the exposed residues and C-terminus, in- cluding secondary structure transition from α-helices to turns in residues 105-110. However, no noticeable changes were observed in the secondary structure of lysozyme during the simulations. Subsequently, molecular mechanics (MM) simulations were carried out to determine the preferred orientation for adsorption of these proteins at poly (ethylene oxide) (PEO) films capped with hydroxyl and methoxy end-groups, based on the Lenard- Jones (L-J) potential. Both proteins preferred to initially adsorb at hy- drophilic surface with its side-on orientation which clef faces sideways. At hydrophobic surface, the preferred orientation of lysozyme became a back- on orientation which clef faces outward, whereas that of apo-α-lactalbumin remained a side-on orientation.

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  • Degree
    Master of Science
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