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Updated: Aug 10, 2026

Solid-phase Submonomer Synthesis of Peptoid Polymers and their Self-Assembly into Highly-Ordered Nanosheets
Published on: November 2, 2011
Promotion of sheet formation in alpha-peptide strands by a beta-peptide reverse turn
B R Huck1, J D Fisk, S H Gellman
1Department of Chemistry and Graduate Program in Biophysics, University of Wisconsin, Madison 53706, USA.
Abstract:
[structure: see text]We show that a tetrapeptide with a heterogeneous backbone, i.e., with two different classes of amino acid residues, adopts a hairpin conformation in which each type of residue plays a different structural role. The alpha-residues at the ends form hydrogen bonds characteristic of antiparallel beta-sheet secondary structure, while the central di-beta-peptide segment forms a reverse turn. The configuration of the turn residues is critical to sheet formation.
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