Disruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn
| Title | Disruption of native beta-turns: consequence of folding competition between native and orthanilic acid proline-based pseudo beta-turn |
| Publication Type | Journal Article |
| Year of Publication | 2016 |
| Authors | Ingole, TS, Vijayadas, KN, Chaitanya, KN, Kotmale, AS, Gawade, RL, Gonnade, RG, Rajamohanan, PR, Sanjayan, GJ |
| Journal | European Journal of Organic Chemistry |
| Issue | 7 |
| Pagination | 1380-1388 |
| Date Published | MAR |
| ISSN | 1434-193X |
| Keywords | Conformation 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. |
| DOI | 10.1002/ejoc.201501558 |
| Type of Journal (Indian or Foreign) | Foreign |
| Impact Factor (IF) | 3.068 |