Perfluoro-tert-butyl-homoserine as a sensitive 19F NMR reporter for peptide–membrane interactions in solution
Article first published online: 19 MAR 2013
Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Volume 19, Issue 5, pages 308–314, May 2013
How to Cite
Buer, B. C., Levin, B. J. and Marsh, E. N. G. (2013), Perfluoro-tert-butyl-homoserine as a sensitive 19F NMR reporter for peptide–membrane interactions in solution. J. Peptide Sci., 19: 308–314. doi: 10.1002/psc.2501
- Issue published online: 15 APR 2013
- Article first published online: 19 MAR 2013
- Manuscript Accepted: 1 FEB 2013
- Manuscript Revised: 31 JAN 2013
- Manuscript Received: 17 DEC 2012
- fluorine NMR;
- antimicrobial peptide;
- fluorinated protein;
Fluorine (19F) NMR is a valuable tool for studying dynamic biological processes. However, increasing the sensitivity of fluorinated reporter molecules is a key to reducing acquisition times and accessing transient biological interactions. Here, we evaluate the utility a novel amino acid, l-O-(perfluoro-t-butyl)-homoserine (pFtBSer), that can easily be synthesized and incorporated into peptides and provides greatly enhanced sensitivity over currently used 19F biomolecular NMR probes. Incorporation of pFtBSer into the potent antimicrobial peptide MSI-78 results in a sharp 19F NMR singlet that can be readily detected at concentrations of 5 µm and lower. We demonstrate that pFtBSer incorporation into MSI-78 provides a sensitive tool to study binding through 19F NMR chemical shift and nuclear relaxation changes. These results establish future potential for pFtBSer to be incorporated into various proteins where NMR signal sensitivity is paramount, such as in-cell investigations. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.