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

  • Author(s) / Creator(s)
  • 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
  • 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.
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  • Citation for previous publication
    • Liu, L., Jalili, N., Baergen, A., Ng, S., Bailey, J., Derda, R., & Klassen, J. S. (2014). Fluorine bonding enhances the energetics of protein-lipid binding in the gas phase. Journal of the American Society for Mass Spectrometry, 25(5), 751-757. http://doi.org/10.1007/s13361-014-0837-8
  • Link to related item
    http://doi.org/10.1007/s13361-014-0837-8