Conformational studies of peptides containing cis-3-hydroxy-D-proline.
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 beta-hairpin structure in both CDCl(3) and DMSO-d(6). Even after the removal of the Bn group, the resulting deprotected compound retained the same structure as in the protected version in CDCl(3). However, in polar solvent DMSO-d(6), the C-terminal strand of the hydroxyl-deprotected peptide flipped to the side of the hydroxyl group, breaking the hairpin to form a pseudo beta-turn-like nine-membered ring structure involving an intramolecular hydrogen bond between LeuNH --> HypC3-OH.
Indian Institute of Chemical Technology, Hyderabad 500 007, India. chakraborty@iict.ap.nic.in
T K
TK
Chakraborty
P
P
Srinivasu
R Vengal
RV
Rao
S Kiran
SK
Kumar
A C
AC
Kunwar
D006909:Hydroxyproline / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008968:Molecular Conformation; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000031:analogs & derivatives* / Q000737:chemistry*
D010455:Peptides; C026215:3-hydroxyproline; D011392:Proline; D006909:Hydroxyproline