Volume 36, Issue 5 pp. 659-667

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Conformational studies of retro–inverso peptides: The crystal and molecular structure of the hydantoin from H-Ala-G-Ala-mGly-OBzl

Ettore Benedetti,

Ettore Benedetti

Biocrystallography Research Center, CNR Department of Chemistry University of Naples “Federico II” 80134 Naples, Italy

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Emilia M Pedone,

Emilia M Pedone

Biocrystallography Research Center, CNR Department of Chemistry University of Naples “Federico II” 80134 Naples, Italy

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Noriyuki H Kawahata,

Noriyuki H Kawahata

Department of Chemistry and Biochemistry University of California San Diego, La Jolla, CA 92093

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Murray Goodman,

Murray Goodman

Department of Chemistry and Biochemistry University of California San Diego, La Jolla, CA 92093

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Ettore Benedetti,

Ettore Benedetti

Biocrystallography Research Center, CNR Department of Chemistry University of Naples “Federico II” 80134 Naples, Italy

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Emilia M Pedone,

Emilia M Pedone

Biocrystallography Research Center, CNR Department of Chemistry University of Naples “Federico II” 80134 Naples, Italy

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Noriyuki H Kawahata,

Noriyuki H Kawahata

Department of Chemistry and Biochemistry University of California San Diego, La Jolla, CA 92093

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Murray Goodman,

Murray Goodman

Department of Chemistry and Biochemistry University of California San Diego, La Jolla, CA 92093

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First published: November 1995

https://doi.org/10.1002/bip.360360511

Citations: 10

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Abstract

The crystal structure of the hydantoin 1-[(S)-1′–aminoethylmalonyl benzyl ester]-(S)-4-methylimidazolidin-2.5-dione (1) derived from the peptide H-Ala-gAla-mGly-OBzl, Having the retro-inverso modification of the Ala-Gly bond, has been determined by x-ray diffraction analysis. The crystals are orthorhombic, space group P2₁2₁2₁ with a = 6.539. b = 14.721, c = 17.101 Å, z = 4. The structure was solved by direct methods and refined with anisotropic thermal factors to a final R value of 0.067 for the 947 observed reflections.

Reversal of the Ala-Gly amide bond perturbs the folding tendency of the backbone shown by the parent peptide t-BuCO-Ala-Gly-NHiPr. The gem-diamino residue, gAla, and the malonyl moieties are found in the helical and the extended conformations, respectively. Intramolecular hydrogen bonding is not observed. The molecules in the crystal are held together by the formation of two intermolecular hydrogen bonds of the NHOC type with NO distances of 2.86 and 3.17 Å respectively. 1995 John Wiley&Sons. Inc. © 1995 John Wiley & Sons, Inc.

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Volume36, Issue5

November 1995

Pages 659-667

Conformational studies of retro–inverso peptides: The crystal and molecular structure of the hydantoin from H-Ala-G-Ala-mGly-OBzl

Abstract

References

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References

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Conformational studies of retro–inverso peptides: The crystal and molecular structure of the hydantoin from H-Ala-G-Ala-mGly-OBzl

Abstract

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