| Abstract
| - In this paper, we present 1,2,3-triazole ε2-amino acids incorporated as a dipeptide surrogate at three positions in the sequence of a known α-helical coiled coil. Biophysical characterization indicates that the modified peptides retain much of the helical structure of the parent sequence, and that the thermodynamic stability of the coiled coil depends on the position of the incorporation of the ε-residue. Crystal structures obtained for each peptide give insight into the chemical behavior and conformational preferences of the non-natural amino acid and show that the triazole ring can participate in the backbone hydrogen bonding of the α-helix as well as template an interhelical crossing between chains in the bundle.
|
