Solid-state and solution-phase conformations of pseudoproline-containing dipeptides

Jack K. Clegg, James R. Cochrane, Nima Sayyadi, Danielle Skropeta, Peter Turner, Katrina A. Jolliffe

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

The conformations of 14 threonine-derived pseudoproline-containing dipeptides (including four d-allo-Thr derivatives) have been investigated by NMR. In solution, the major conformer observed for all dipeptides is that in which the amide bond between the pseudoproline and the preceding amino acid is cis. For dipeptides in which the N-terminus is protected, the ratio of cis- to trans-conformers does not depend significantly on the side chain of the N-terminal amino acid, or the stereochemistry of the Thr residue. However, for dipeptides bearing a free N-terminus, there are significant differences in the ratios of cis- to trans-conformers depending on the side chain present. Three dipeptides were crystallized and their X-ray structures determined. In two cases, (benzyloxycarbonyl (Cbz)-Val-Thr(Me,Mepro)-OMe and Cbz-Val-Thr(Me,Mepro)-OH), the dipeptides adopt a trans-conformation in the solid state, in contrast to the structures observed in solution. In the third case, (9-fluorenylmethoxycarbonyl (Fmoc)-Val-d-allo-Thr( Me,Mepro)-OH), a cis-amide geometry is observed. These structural differences are attributed to crystal-packing interactions.

Original languageEnglish
Pages (from-to)711-719
Number of pages9
JournalAustralian Journal of Chemistry
Volume62
Issue number7
DOIs
Publication statusPublished - 2009
Externally publishedYes

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