Crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate. Unusual conformational characteristics of a cyclic hexapeptide

M. Czugler, Kálmán Sasvári, M. Hollósi

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Abstract

The crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate, C24H34O6N6·3H2O, has been determined from single-crystal X-ray diffraction data. The phase problem was solved by direct methods. The space group is P212121 with the dimensions a = 9.237 (4) Å, b = 13.972 (3) Å, c = 20.851 (3) Å, and Z = 4. The synthetic hexapeptide contains one transannular intramolecular C=O⋯NH hydrogen bond. In combination with three molecules of water, a coherent system of hydrogen bonds is formed in which also an intermolecular bifurcated hydrogen bond is present. Thus in the lattice parallel to the b axis, linear molecular chains are formed. The peptide backbone contains one cis Gly-Pro and one cis Pro-Pro linkage in consecutive positions. The most striking feature of the asymmetric conformation is, however, the occurrence of a hydrogen-bonded type I β-turn encompassing two trails-configured proline residues in the other half of the molecule. Concerning these linkages, the conformation of the cyclic hexapeptide in the present crystal differs from that in its Mg2+ complex.

Original languageEnglish
Pages (from-to)4465-4469
Number of pages5
JournalJournal of the American Chemical Society
Volume104
Issue number16
Publication statusPublished - 1982

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Hydrogen
Hydrogen bonds
Crystal structure
Conformations
Molecules
glycylproline
Proline
Peptides
X-Ray Diffraction
Single crystals
X ray diffraction
Crystals
Water
cyclo(glycylprolyl)
poly(prolylprolylglycine)15

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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title = "Crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate. Unusual conformational characteristics of a cyclic hexapeptide",
abstract = "The crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate, C24H34O6N6·3H2O, has been determined from single-crystal X-ray diffraction data. The phase problem was solved by direct methods. The space group is P212121 with the dimensions a = 9.237 (4) {\AA}, b = 13.972 (3) {\AA}, c = 20.851 (3) {\AA}, and Z = 4. The synthetic hexapeptide contains one transannular intramolecular C=O⋯NH hydrogen bond. In combination with three molecules of water, a coherent system of hydrogen bonds is formed in which also an intermolecular bifurcated hydrogen bond is present. Thus in the lattice parallel to the b axis, linear molecular chains are formed. The peptide backbone contains one cis Gly-Pro and one cis Pro-Pro linkage in consecutive positions. The most striking feature of the asymmetric conformation is, however, the occurrence of a hydrogen-bonded type I β-turn encompassing two trails-configured proline residues in the other half of the molecule. Concerning these linkages, the conformation of the cyclic hexapeptide in the present crystal differs from that in its Mg2+ complex.",
author = "M. Czugler and K{\'a}lm{\'a}n Sasv{\'a}ri and M. Holl{\'o}si",
year = "1982",
language = "English",
volume = "104",
pages = "4465--4469",
journal = "Journal of the American Chemical Society",
issn = "0002-7863",
publisher = "American Chemical Society",
number = "16",

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TY - JOUR

T1 - Crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate. Unusual conformational characteristics of a cyclic hexapeptide

AU - Czugler, M.

AU - Sasvári, Kálmán

AU - Hollósi, M.

PY - 1982

Y1 - 1982

N2 - The crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate, C24H34O6N6·3H2O, has been determined from single-crystal X-ray diffraction data. The phase problem was solved by direct methods. The space group is P212121 with the dimensions a = 9.237 (4) Å, b = 13.972 (3) Å, c = 20.851 (3) Å, and Z = 4. The synthetic hexapeptide contains one transannular intramolecular C=O⋯NH hydrogen bond. In combination with three molecules of water, a coherent system of hydrogen bonds is formed in which also an intermolecular bifurcated hydrogen bond is present. Thus in the lattice parallel to the b axis, linear molecular chains are formed. The peptide backbone contains one cis Gly-Pro and one cis Pro-Pro linkage in consecutive positions. The most striking feature of the asymmetric conformation is, however, the occurrence of a hydrogen-bonded type I β-turn encompassing two trails-configured proline residues in the other half of the molecule. Concerning these linkages, the conformation of the cyclic hexapeptide in the present crystal differs from that in its Mg2+ complex.

AB - The crystal structure of cyclo-(Gly-L-Pro-L-Pro-Gly-L-Pro-L-Pro) trihydrate, C24H34O6N6·3H2O, has been determined from single-crystal X-ray diffraction data. The phase problem was solved by direct methods. The space group is P212121 with the dimensions a = 9.237 (4) Å, b = 13.972 (3) Å, c = 20.851 (3) Å, and Z = 4. The synthetic hexapeptide contains one transannular intramolecular C=O⋯NH hydrogen bond. In combination with three molecules of water, a coherent system of hydrogen bonds is formed in which also an intermolecular bifurcated hydrogen bond is present. Thus in the lattice parallel to the b axis, linear molecular chains are formed. The peptide backbone contains one cis Gly-Pro and one cis Pro-Pro linkage in consecutive positions. The most striking feature of the asymmetric conformation is, however, the occurrence of a hydrogen-bonded type I β-turn encompassing two trails-configured proline residues in the other half of the molecule. Concerning these linkages, the conformation of the cyclic hexapeptide in the present crystal differs from that in its Mg2+ complex.

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