Kinins pp 43-51 | Cite as

Conformation of Bradykinin in Relation to Solvent Environment

  • D. I. Marlborough
  • J. W. Ryan
  • A. M. Felix
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 70)


For a small peptide, bradykinin has an unusually large percentage of proline residues in its primary structure. The occurrence of proline in a peptide chain tends to restrict the conformational flexibility of the peptide (1). Bradykinin would therefore be expected to show some degree of ordered structure in solution. Early optical rotatory dispersion (ORD) and circular dichroism (CD) results (2,3), however, suggested that the structure was freely flexible in aqueous solution. Later CD measurements on bradykinin and some of its homologs in aqueous and non-aqueous solvents (4) were interpreted as showing partial intramolecular hydrogenbonding. An 8 → 6 hydrogen-bond across proline7 was postulated for bradykinin in aqueous solution, while additional 9 → 7 and 4 → 2 hydrogen-bonds across phenylalanine8 and proline3 respectively were postulated in dioxane solution. The model on which Cann’s conclusions are based is an intramolecularly hydrogen-bonded proline derivative in non-aqueous solvents. In non-aqueous solvents the possibility of other intramolecular interactions and solvent interaction with the peptide is minimized. It seems likely therefore, that the model for bradykinin in aqueous solution would be complicated by the possible interactions described above.


Circular Dichroism Circular Dichroism Spectrum Guanidine Hydrochloride Circular Dichroism Measurement Solvent Environment 


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Copyright information

© Plenum Press, New York 1976

Authors and Affiliations

  • D. I. Marlborough
    • 1
  • J. W. Ryan
    • 1
  • A. M. Felix
    • 2
  1. 1.Papanicolaou Cancer Research InstituteMiamiUSA
  2. 2.Hoffmann-La Roche Inc.NutleyUSA

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