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The solid state and solution phase conformational preferences of a homologous series of β-peptides derived from (S,S)-2- aminocyclopentanecarboxylic acid (transpentacin) have been investigated using a variety of spectroscopic and crystallographic techniques. These studies indicate that the hexamer and pentamer persist as a 12-helix in both the solid state and solution phase. Although the conformational traits of a 12-helix are exhibited by oligomers with as few as three residues in the solid state, in solution the trimer exists as an equilibrium of many alternative conformers whilst the tetramer has been shown to predominantly exist in either a 12-helix or a turn-type conformation. © 2010 Elsevier Ltd. All rights reserved.

Original publication

DOI

10.1016/j.tetasy.2010.06.001

Type

Journal article

Journal

Tetrahedron Asymmetry

Publication Date

14/07/2010

Volume

21

Pages

1797 - 1815