ORGN 128 |
| Highly fluorinated amino acids have been used to stabilize helical motifs, however minimal studies have been performed on sheet-containing proteins. In this presentation, we measured the beta-sheet propensity using the protein G B1 domain for various amino acids: pentafluorophenylalanine, 5,5,5,5',5',5'-hexafluoroleucine, 5,5,5',5'-tetrafluoroleucine, phenylalanine, leucine, alanine, and glycine. The corresponding 56-residue proteins were synthesized by solid phase peptide synthesis using Fmoc-based chemistry. Thermal denaturation of these proteins were monitored by circular dichroism spectroscopy. The denaturation of all proteins was fully reversible. Interestingly, fluorinated amino acids favor beta-sheet formation over their corresponding hydrocarbon amino acids. Furthermore, pentafluorophenylalanine was the most beta-sheet stabilizing amino acid. These results suggest that highly fluorinated amino acids may be useful for stabilizing beta-sheet-containing proteins. |
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Total Synthesis, Materials, Devices and Switches, Molecular Recognition and Self-Assembly, Biologically-Related Molecules and Processes
8:00 PM-10:00 PM, Sunday, August 19, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Organic Chemistry |