Disruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn

TitleDisruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn
Publication TypeJournal Article
Year of Publication2016
AuthorsIngole, TS, Vijayadas, KN, Chaitanya, KN, Kotmale, AS, Gawade, RL, Gonnade, RG, Rajamohanan, PR, Sanjayan, GJ
JournalEuropean Journal of Organic Chemistry
Issue7
Pagination1380-1388
Date PublishedMAR
ISSN1434-193X
KeywordsConformation analysis, hydrogen bonds, Peptidomimetics, structure elucidation
Abstract

Five tetrapeptides comprising beta-turn-forming elements and a pseudo beta-turn (C9 H-bonding) based on an SAntPro (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 beta-turn (C10 H-bonding) architecture. The striking difference between the psi(psi(2)) angle of ``i + 2'' residues of native beta-turn and designed peptides suggest that formation of the native beta-turn is not favored. The results suggest that other turn-forming motifs can dramatically modulate the stability of the native beta-turn structure.

DOI10.1002/ejoc.201501558
Type of Journal (Indian or Foreign)

Foreign

Impact Factor (IF)

3.068

Divison category: 
Center for Material Characterization (CMC)
Central NMR Facility
Organic Chemistry