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beta -Helical polymers from isocyanopeptides.

J J Cornelissen·J J Donners·R de Gelder·W S Graswinckel·G A Metselaar·A E Rowan·N A Sommerdijk·R J 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 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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AlanineCircular DichroismCyanidesHydrogen BondingMagnetic Resonance SpectroscopyMicroscopy, Atomic ForceMolecular ConformationOligopeptidesPeptidesPolymersProtein FoldingProtein Structure, SecondarySpectrophotometry, InfraredTemperatureTrifluoroacetic AcidWaterJournal ArticleResearch Support, Non-U.S. Gov't

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J J Cornelissen, J J Donners, R de Gelder, W S Graswinckel, G A Metselaar, A E Rowan, N A Sommerdijk, R J Nolte. 2001-07-27. beta -Helical polymers from isocyanopeptides.. https://doi.org/10.1126/science.1062224

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