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Backbone side-chain interactions in peptides

IV. β-Turn conformations of Asp and Asn-containing dipeptides in solute and solid states

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IR, 1H-NMR and X-ray experiments have been carried out on dipeptides with the Pro-Asp and Pro-Asn sequences protected on both ends by amide groups. The Pro-Asp dipeptide was investigated for the carboxylic, methyl ester and carboxylate forms of the Asp residue.

In solution, all dipeptides are found to accommodate almost exclusively the βI-turn conformation stabilized by an interaction between the Asp or Asn-NH and CγO bonds. The βI-turn percentage roughly parallels the basicity of the Asp or Asn side substituent, and decreases from Asp- to Asn, and to Asp or Asp (OMe).

The βI-turn, stabilized by the interaction involving the Asp-CγO site, is retained in the crystal structure of the Pro-Asp(OMe) dipeptide. The Pro-Asp and Pro-Asn dipeptides assume a βII-turn conformation in the solid state and the polar Asp or Asn side-groups are involved in a complex network of intermolecular interactions.

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Correspondence to M. Marraud.

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Mcharfi, M., Aubry, A., Boussard, G. et al. Backbone side-chain interactions in peptides. Eur Biophys J 14, 43–51 (1986). https://doi.org/10.1007/BF00260402

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Key words

  • β-bend
  • crystal structure
  • hydrogen bond
  • infrared spectroscopy
  • NMR spectroscopy
  • peptide conformation
  • X-ray diffraction