Water-soluble polypeptides adopting a-helical conformations with unprecedented high helicities were obtained by elongating the charge-containing side chains of the constituent amino acids to allow the terminal charges to be situated distally from the peptide backbone. Poly(?-(4-aminoethylthiopropoxyl)-benzyl-L-glutamate) with a charge-peptide backbone distance of 17 s-bonds exhibited a remarkably high helicity (81%) at a degree of polymerization of 10. The helical conformations of these short polypeptides were very stable against various harsh, protein-denaturing conditions, such as extreme pH, high temperature, and high salt or urea concentrations.Scheme.  Chemical structure of PAOBLG-AET with an elongating the charge-containing side chains and the postulated helix structure.

Ultra-stable helical, water-soluble polypeptides with elongated, charged side chains

243rd National Meeting (2012)

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