beta-helical polymers from isocyanopeptides

Polymerization of isocyanopeptides results in the formation of high molecul ar mass polymers that fold in a proteinlike fashion to give helical strands in which the peptide chains are arranged in beta -sheets. The beta -helica l polymers retain their structure in water and unfold in a cooperative proc ess 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 cor e that acts as a director for the beta -sheet-like arrangement of the pepti de side arms. The helical structure of these isocyanopeptide polymers has t he potential to be controlled through tailoring of the side branches and th e hydrogen-bonding network present in the beta -sheets.