Fluorine bonding enhances the energetics of protein-lipid binding in the gas phase

• Author(s) / Creator(s)

  • Klassen, John S.
  • Ng, Simon
  • Liu, Lan
  • Bailey, Justin
  • Derda, Ratmir
  • Baergen, Alyson
  • Jalili, Nobar

• This paper reports on the first experimental study of the energies of noncovalent fluorine bonding in a protein-ligand complex in the absence of solvent. Arrhenius parameters were measured for the dissociation of gaseous deprotonated ions of complexes of bovine β-lactoglobulin (Lg), a model lipid-binding protein, and four fluorinated analogs of stearic acid (SA), which contained (X =) 13, 15, 17, or 21 fluorine atoms. In all cases, the activation energies (Ea) measured for the loss of neutral XF-SA from the (Lg + XF-SA)7– ions are larger than for SA. From the kinetic data, the average contribution of each > CF2 group to Ea was found to be ~1.1 kcal mol–1, which is larger than the ~0.8 kcal mol–1 value reported for > CH2 groups. Based on these results, it is proposed that fluorocarbon–protein interactions are inherently stronger (enthalpically) than the corresponding hydrocarbon interactions.

• Date created

  2014

• Subjects / Keywords

  • Hydrophobic interactions
  • Fluorine bonding
  • Molecular recognition
  • Energetics
  • Protein-ligand complexes

• Type of Item

  Article (Published)

• DOI

  https://doi.org/10.7939/R3XS5JW0B

• License

  © 2014 Liu, L., Jalili, N., Baergen, A., Ng, S., Bailey, J., Derda, R., & Klassen, J. S. This version of this article is open access and can be downloaded and shared. The original author(s) and source must be cited.