β-Helical Polymers from Isocyanopeptides

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Science  27 Jul 2001:
Vol. 293, Issue 5530, pp. 676-680
DOI: 10.1126/science.1062224

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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 β-sheets. The β-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 β-helix motif found in proteins. Unlike their natural counterparts, which contain arrays of large β-sheets stacked in a helical fashion, the isocyanopeptide polymers have a central helical core that acts as a director for the β-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 β-sheets.

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