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Chemistry of Natural Compounds

, Volume 7, Issue 3, pp 297–306 | Cite as

A study of the conformational states of cyclopeptide systems III. Cyclohexapeptides as systems of interacting amide chromophores

  • V. T. Ivanov
  • G. A. Kogan
  • E. A. Meshcheryakova
  • V. V. Shilin
  • Yu. A. Ovchinnikov
Article

Summary

1. The UV spectra of aqueous solutions of cyclohexapeptides constructed of L(D)-alanine and glycine residues exhibit a considerable (about 45%) hypochromism of the band of the π→π* transition which has hitherto been observed among peptide-protein systems only in α-helical polypeptides.

2. In water, almost all the polypeptides studied have monotypical CD and ORD curves characterized by two Cotton effects of opposite sign in the region of the π→π* transition.

3. The features of the optical properties of the cyclohexapeptides are connected with the exciton interaction of the amide chromophores in the "pleated sheet" conformation. The neglect of such interactions may lead to high results in the determination of the degree of helicity in proteins from CD and ORD observations.

4. On passing to less polar solvents, there is a redistribution of the intensities of the Cotton effects connected with a conformational rearrangement of the cyclohexapeptides.

The authors express their gratitude to Professor E. Scoffone (Institute of Organic Chemistry, University of Padua, Italy) for kindly providing one of us (VTI) with the possibility of performing measurements on Cary-15 and JOUAN 11 instruments.

Keywords

Circular Dichroism Cotton Effect Alanine Residue Chromophoric Group Methylamide 

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Copyright information

© Consultants Bureau, a division of Plenum Publishing Corporation 1973

Authors and Affiliations

  • V. T. Ivanov
  • G. A. Kogan
  • E. A. Meshcheryakova
  • V. V. Shilin
  • Yu. A. Ovchinnikov

There are no affiliations available

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