In:
European Journal of Organic Chemistry, Wiley, Vol. 2016, No. 7 ( 2016-03), p. 1380-1388
Kurzfassung:
Five tetrapeptides comprising β‐turn‐forming elements and a pseudo β‐turn (C9 H‐bonding) based on an S Ant‐Pro (orthanilic acid – proline) motif were designed and synthesized. Their extensive conformational investigation by single‐crystal X‐ray crystallography, solution‐state 2D NMR spectroscopic, and nOe‐restrained MD simulation studies revealed the formation of C14 or C9 folding and disruption of the native β‐turn (C10 H‐bonding) architecture. The striking difference between the ψ ( ψ 2 ) angle of “ i + 2” residues of native β‐turn and designed peptides suggest that formation of the native β‐turn is not favored. The results suggest that other turn‐forming motifs can dramatically modulate the stability of the native β‐turn structure.
Materialart:
Online-Ressource
ISSN:
1434-193X
,
1099-0690
DOI:
10.1002/ejoc.v2016.7
DOI:
10.1002/ejoc.201501558
Sprache:
Englisch
Verlag:
Wiley
Publikationsdatum:
2016
ZDB Id:
1475010-7
