Fluorine bonding enhances the energetics of protein-lipid binding in the gas phase
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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
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http://doi.org/10.1007/s13361-014-0837-8
Abstract
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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.
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http://purl.org/coar/resource_type/c_6501 http://purl.org/coar/version/c_970fb48d4fbd8a85
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© 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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en