beta -Helical Polymers from Isocyanopeptides

doi:10.1126/science.1062224

Account Information

Guest Alerts | Access Rights | My Account | Sign In

Site Navigation

Article Views

Article Tools

My Science

More Information

Related Jobs from ScienceCareers

Science 27 July 2001:
Vol. 293. no. 5530, pp. 676 - 680
DOI: 10.1126/science.1062224

Prev | Table of Contents | Next

Reports

$beta$ -Helical Polymers from Isocyanopeptides

Jeroen J. L. M. Cornelissen,¹ Jack J. J. M. Donners,³ René de Gelder,² W. Sander Graswinckel,¹ Gerald A. Metselaar,¹ Alan E. Rowan,¹ Nico A. J. M. Sommerdijk,³ Roeland J. M. Nolte¹³^*

Polymerization of isocyanopeptides results in the formation of high molecular mass polymers that fold in a proteinlike fashionto give helical strands in which the peptide chains are arrangedin $beta$ -sheets. The $beta$ -helical polymers retain their structure inwater and unfold in a cooperative process at elevated temperatures.The peptide architecture in these polymers is a different formof the $beta$ -helix motif found in proteins. Unlike their natural counterparts,which contain arrays of large $beta$ -sheets stacked in a helical fashion,the isocyanopeptide polymers have a central helical core thatacts as a director for the $beta$ -sheet-like arrangement of the peptideside arms. The helical structure of these isocyanopeptide polymershas the potential to be controlled through tailoring of the sidebranches and the hydrogen-bonding network present in the $beta$ -sheets.

¹ Department of Organic Chemistry,
² Department of Inorganic Chemistry, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, Netherlands.
³ Laboratory for Macromolecular and Organic Chemistry, Eindhoven University of Technology, Post Office Box 513, 5600 MB Eindhoven, Netherlands.
^* To whom correspondence should be addressed. E-mail: nolte{at}sci.kun.nl