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Issue 5, 2015
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Participation of non-aminoisobutyric acid (Aib) residues in the 310 helical conformation of Aib-rich foldamers: a solid state study

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Abstract

The solid state conformational preferences of a series of 2-aminoisobutyric acid (Aib) foldamers bearing a single N-terminal tertiary amino acid (Cbz-L-phenylalanine (Cbz-L-Phe)) have been investigated by X-ray crystallography. The type of β-turn present at the N-terminus and the global screw-sense preferences of the Aib foldamers were determined by analysis of intramolecular hydrogen-bonds and peptide torsion angles. The contrasting influence of a C-terminal ester or amide on the 310 helical conformation of the foldamers was established by identifying the hydrogen-bonding motifs adopted in the solid state. The ability of non-Aib achiral quaternary residues in the middle of the chain to stabilise the 310 helix was similarly confirmed. Combining these structural features, which promote the formation of consecutive ii + 3 β-turns in Aib foldamers, permitted the formation of long chain oligomers in 310 helical conformations that extend over 21 Å.

Graphical abstract: Participation of non-aminoisobutyric acid (Aib) residues in the 310 helical conformation of Aib-rich foldamers: a solid state study

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Supplementary files

Article information


Submitted
10 Sep 2014
Accepted
16 Dec 2014
First published
17 Dec 2014

New J. Chem., 2015,39, 3288-3294
Article type
Paper
Author version available

Participation of non-aminoisobutyric acid (Aib) residues in the 310 helical conformation of Aib-rich foldamers: a solid state study

S. J. Pike, T. Boddaert, J. Raftery, S. J. Webb and J. Clayden, New J. Chem., 2015, 39, 3288
DOI: 10.1039/C4NJ01547A

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