Reversible α-helix formation controlled by a hydrogen bond surrogate.

ABSTRACT: Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized α-helix that utilizes an internal disulfide linkage. Structural analysis indicates that the dynamic nature of the disulfide bridge allows for the reversible formation of an α-helix through oxidation and reduction reactions.

SUBMITTER: Miller SE 

PROVIDER: S-EPMC3490425 | biostudies-literature | 2012 Jun

REPOSITORIES: biostudies-literature