A Cyclic Metallopeptide Induces α Helicity in Short Peptide Fragments of Thermolysin

Abstract

Coordination of [Pd(en)]2+ to histidine residues in 5-, 10-, and 15-residue peptides results in α-helical structures that mimic the Zn2+-binding domain of thermolysin. The novel 22-membered metallacycle 1 (e.g. R1=Ac, R2=NH2) is an α-helix-inducing template. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2003/z19863_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.