Photocontrolled Folding and Unfolding of a Collagen Triple Helix

Abstract

At the flick of a switch: Two side chains of a collagen peptide containing (2S,4S)-mercaptoproline at two defined positions are linked with a diiodo azobenzene derivative. With the trans isomer of the azobenzene clamp (orange), the peptide folds into the collagen triple helix (green, blue, gray), which unfolds upon irradiation at 330 nm. The light-controlled folding/unfolding processes are fully reversible, making this system well-suited for ultrafast spectroscopic analysis. Supporting information for this article is available on the WWW under http://www.wiley-vch.de/contents/jc_2002/2006/z601432_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.