beta -Helical polymers from isocyanopeptides |
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| Authors: | Cornelissen J J Donners J J de Gelder R Graswinckel W S Metselaar G A Rowan A E Sommerdijk N A Nolte R J |
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| Institution: | Department of Organic Chemistry, University of Nijmegen, Toernooiveld 1, 6525 ED Nijmegen, Netherlands. |
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| Abstract: | 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. |
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