Sequence-specific polypeptoids: A diverse family of heteropolymers with stable secondary structure

Kent Kirshenbaum, Annelise E. Barron, Richard A. Goldsmith, Philippe Armand, Erin K. Bradley, Kiet T.V. Truong, Ken A. Dill, Fred E. Cohen, Ronald N. Zuckermann

Research output: Contribution to journalArticlepeer-review

Abstract

We have synthesized and characterized a family of structured oligo-N- substituted-glycines (peptoids) up to 36 residues in length by using an efficient solid-phase protocol to incorporate chemically diverse side chains in a sequence-specific fashion. We investigated polypeptoids containing side chains with a chiral center adjacent to the main chain nitrogen. Some of these sequences have stable secondary structure, despite the achirality of the polymer backbone and its lack of hydrogen bond donors. In both aqueous and organic solvents, peptoid oligomers as short as five residues give rise to CD spectra that strongly resemble those of peptide α-helices. Differential scanning calorimetry and CD measurements show that polypeptoid secondary structure is highly stable and that unfolding is reversible and cooperative. Thermodynamic parameters obtained for unfolding are similar to those obtained for the α-helix to coil transitions of peptides. This class of biomimetic polymers may enable the design of self-assembling macromolecules with novel structures and functions.

Original languageEnglish (US)
Pages (from-to)4303-4308
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume95
Issue number8
DOIs
StatePublished - Apr 14 1998

ASJC Scopus subject areas

  • General

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