Dynamic Covalent Chemistry on Self‐Templating Peptides: Formation of a Disulfide‐linked β‐Hairpin Mimic

Driving peptides round the bend: Thiol-containing linear peptides (ASH and BSH) are dimerized (see scheme) using dynamic covalent chemistry to preferentially form an energetically stabilized disulfide by a self-templating mechanism. NMR spectroscopy experiments on this disulfide show that the stabilization is a result of β-sheet formation with the disulfide bond acting as a turn scaffold yielding a peptide with a hairpin-type conformation. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2003/z50551_s.pdf or from the author. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.