Crystal structure analysis of a beta-turn mimic in hydrazino peptides.
The crystal structures of four hydrazino peptides (Piv-Pro-h(N alpha-Bzl)Gly-NHiPr 1, Piv-Pro-hAla-NHiPr 2, Moc-hPro-NHiPr 3, and Boc-hPro-Gly-N(OH)Me 4) deriving from the hydrazino analogues of glycine (hGly), L-alanine (hAla) or L-proline (hPro) have been solved. They reveal a common folded structure of the alpha-hydrazino acid residue characterized by a bifurcated hydrogen bond closing an eight-membered cycle. This folded structure is topologically similar to the beta II'-turn in peptides, and the CO-NH-N hydrazide link can be considered as a good turn-inducer in peptide analogues.
Aubry
A
A
CNRS-URA-809, University of Nancy I, Vandoeuvre, France.
Mangeot
J P
JP
Vidal
J
J
Collet
A
A
Zerkout
S
S
Marraud
M
M
D006834:Hydrazines / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014961:X-Ray Diffraction
D006834:Hydrazines; D010455:Peptides