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.

• Subjects / Keywords

  • Apo-α-Lactalbumin
  • Protein adsorption
  • Adsorption orientation
  • Stability
  • Lysozyme

• Graduation date

  Fall 2012

• Type of Item

  Thesis

• Degree

  Master of Science

• DOI

  https://doi.org/10.7939/R36403

• License

  This thesis is made available by the University of Alberta Libraries with permission of the copyright owner solely for non-commercial purposes. This thesis, or any portion thereof, may not otherwise be copied or reproduced without the written consent of the copyright owner, except to the extent permitted by Canadian copyright law.