We report the first successful design of a self-associating antiparallel coiled coil, APH. The simultaneous application of Coulombic and hydrophobic components results in a decided preference for the antiparallel alignment as judged by HPLC, sedimentation equilibrium, and chemical denaturation data. The designed peptide is of comparable stability to naturally occurring leucine zipper peptides and can be expressed in bacteria. These properties of APH suggest potential in vivo protein fusion and biomaterials applications.
|Original language||English (US)|
|Number of pages||2|
|Journal||Journal of the American Chemical Society|
|State||Published - Jun 25 2003|
ASJC Scopus subject areas
- Colloid and Surface Chemistry