4.4 Article

Reversible α-helix formation controlled by a hydrogen bond surrogate

Journal

TETRAHEDRON
Volume 68, Issue 23, Pages 4434-4437

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.tet.2011.12.068

Keywords

Foldamer; Stabilized alpha-helix; Helix inducer; Hydrogen bond surrogate; Disulfide bridge

Funding

  1. National Science Foundation [CHE1027009, CHE-0958457]
  2. National Institutes of Health [GM073943]
  3. New York University Department of Chemistry
  4. Division Of Chemistry
  5. Direct For Mathematical & Physical Scien [0958457, 1027009] Funding Source: National Science Foundation

Ask authors/readers for more resources

Strategically placed covalent linkages have been shown to stabilize helical conformations in short peptide sequences. Here we report the synthesis of a stabilized alpha-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 alpha-helix through oxidation and reduction reactions. (C) 2011 Elsevier Ltd. All rights reserved.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.4
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available