The Synthesis and Characterization of a Pentafluorosulfanylated Peptide

The design and synthesis of pentafluorosulfanyl-containing heptad amino acid sequence was described. The three-dimensional conformation of the peptide was investigated by using CYANA (combined assignment and dynamics algorithm for NMR applications) and the integrated autoassignment. This study shows that the one of the diastereomers assumed a very tight coiled conformation in [D6]DMSO where both pentafluorosulfanyl groups assumed a synclinal relationship. The propensity of the protected heptapeptide to form such a tight coil and of the pentafluorosulfanyl groups to align so uniformly is suggestive of the utility of pentafluorosulfanylated amino acids in promoting conformational control.