Sequence‐Based Design of α/β‐Peptide Foldamers That Mimic BH3 Domains

Abstract

Into the fold: Foldamers have emerged as versatile scaffolds for the design of functional macromolecules. A straightforward design principle based on primary sequence can be used to convert an α-peptide ligand derived from a natural protein-binding domain into an α/β-peptide with comparable binding affinity for protein targets bound by the α-peptide (see scheme). Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2008/z705315_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.