Peptoids, oligomeric N-substituted glycines, are a class of foldamers that possess the potential to adopt well defined secondary structures, making them attractive for use as biomimetics.  Peptoids have been shown to be capable of adopting a helical conformation similar to a polyproline type I (PP-I) helix, and studies have shown that stable peptoid helices are promoted by inclusion of at least 50% N-a-chiral side chains, an a-chiral substituent at the C-terminus, and aromatic residues at i and i+3 positions.  While the structures of peptoid helices with phenylethyl side chains have been well studied, the 1-naphthylethyl side chain is suggested to be more strongly helix promoting. Peptoid helices comprising this residue have recently been studied in the solid state and in organic solvents.  In order for peptoids to be incorporated into a biological system, however, it must be water soluble.  Thus, our research lab has incorporated the 1-naphthylethyl side chain into water soluble peptoids and is investigating its structure related effects using a range of biophysical techniques.

Structural studies of self-associating water-soluble peptoids

247th National Meeting (2014)

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