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Science 27 July 2001:
Vol. 293. no. 5530, pp. 676 - 680
DOI: 10.1126/science.1062224
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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 fashion to give helical strands in which the peptide chains are arranged in beta -sheets. The beta -helical polymers retain their structure in water and unfold in a cooperative process at elevated temperatures. The peptide architecture in these polymers is a different form of 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 that acts as a director for the beta -sheet-like arrangement of the peptide side arms. The helical structure of these isocyanopeptide polymers has the potential to be controlled through tailoring of the side branches 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

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Science. ISSN 0036-8075 (print), 1095-9203 (online)