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. 1990 Sep 1;270(2):313–318. doi: 10.1042/bj2700313

Conformational studies of peptides corresponding to the coeliac-activating regions of wheat alpha-gliadin.

A S Tatham 1, M N Marsh 1, H Wieser 1, P R Shewry 1
PMCID: PMC1131722  PMID: 2400392

Abstract

The structures of four peptides corresponding to parts of the coeliac-activating protein A-gliadin were studied by structure prediction and c.d. spectroscopy. Three of the peptides corresponded to parts of the coeliac-activating N-terminal region (residues 3-55, 3-19 and 39-45) and contained two tetrapeptide motifs common to all coeliac-active regions (Pro-Ser-Gln-Gln and Gln-Gln-Gln-Pro). The Pro-Ser-Gln-Gln sequence was also present in the fourth peptide, on the basis of the C-terminal part of the molecule (211-217). These studies showed that beta-reverse turns were the predominant structural feature in all peptides and were predominantly of type I/III in two of the N-terminal peptides and type II in the C-terminal peptide. These turns form when the peptide is dissolved in solvents of low dielectric constant (trifluoroethanol) and high dielectric constant (water and iso-osmotic saline), although their presence in the N-terminal peptides may be masked in the latter solvents due to equilibrium with a poly-L-proline II structure favoured at lower temperatures.

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Selected References

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