Beta-helical polymers from isocyanopeptides

J.J.L.M. Cornelissen, J.J.J.M. Donners, R. Gelder, de, W.S. Graswinckel, G.A. Metselaar, A.E. Rowan, N.A.J.M. Sommerdijk, R.J.M. Nolte

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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 ß-sheets. The ß-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 ß-helix motif found in proteins. Unlike their natural counterparts, which contain arrays of large -sheets stacked in a helical fashion, the isocyanopeptide polymers have a central helical core that acts as a director for the ß-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 ß-sheets.
Original languageEnglish
Pages (from-to)676-680
JournalScience
Volume293
Issue number5530
DOIs
Publication statusPublished - 2001

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