Fluorine Bonding Enhances the Energetics of Protein-Lipid Binding in the Gas Phase

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

DOI: 10.1007/s13361-014-0837-8

Cite this article as:
Liu, L., Jalili, N., Baergen, A. et al. J. Am. Soc. Mass Spectrom. (2014) 25: 751. doi:10.1007/s13361-014-0837-8

Abstract

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.

Key words

Protein-ligand complexes Fluorine bonding Hydrophobic interactions Molecular recognition Energetics 

Supplementary material

13361_2014_837_MOESM1_ESM.doc (2.7 mb)
ESM 1(DOC 2763 kb)

Copyright information

© American Society for Mass Spectrometry 2014

Authors and Affiliations

  • Lan Liu
    • 1
  • Nobar Jalili
    • 1
  • Alyson Baergen
    • 1
  • Simon Ng
    • 1
  • Justin Bailey
    • 1
  • Ratmir Derda
    • 1
  • John S. Klassen
    • 1
  1. 1.Alberta Glycomics Centre and Department of ChemistryUniversity of AlbertaEdmontonCanada

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