Conformational studies of peptides containing cis-3-hydroxy-D-proline

Chakraborty, T. K. ; Srinivasu, P. ; Vengal Rao, R. ; Kiran Kumar, S. ; Kunwar, A. C. (2004) Conformational studies of peptides containing cis-3-hydroxy-D-proline Journal of Organic Chemistry, 69 (21). pp. 7399-7402. ISSN 0022-3263

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Conformational analysis of peptides containing cis-3-hydroxy-D-proline (D-cis-3-Hyp) by NMR studies revealed that the 3-hydroxyl group in this amino acid plays a significant role in the overall three-dimensional structures of the peptides. When the D-cis-3-Hyp had its 3-hydroxyl group protected as the benzyl (Bn) ether, the peptide displayed a β-hairpin structure in both CDCl3 and DMSO-d6. Even after the removal of the Bn group, the resulting deprotected compound retained the same structure as in the protected version in CDCl3. However, in polar solvent DMSO-d6, the C-terminal strand of the hydroxyl-deprotected peptide flipped to the side of the hydroxyl group, breaking the hairpin to form a pseudo β-turn-like nine-membered ring structure involving an intramolecular hydrogen bond between LeuNH → HypC3-OH.

Item Type:Article
Source:Copyright of this article belongs to American Chemical Society.
ID Code:20562
Deposited On:20 Nov 2010 14:18
Last Modified:22 May 2011 15:04

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