Is the C-terminal region of bradykinin the binding site of polyphenols?

J Biomol Struct Dyn. 2003 Dec;21(3):379-85. doi: 10.1080/07391102.2003.10506933.

Abstract

Bradykinin is a bioactive hormone involved in a variety of physiological processes. In various solvents, this peptide adopts beta-turn structures. The C-terminal turn is a structural feature for the receptor affinity of agonists and antagonists while the N-terminal turn might be important for antagonistic activities. Polyphenols like dimeric proanthocyanidin B3 interact with the peptide. Thus to investigate the effects of polyphenols on bradykinin activity and structure, we studied the interaction in the structuring solvent DMSO which can be a close mimic of aqueous physiological environments like receptor-binding sites. Bradykinin alone presented a folded structure with two turns. B3 interacted with the peptide C-terminus and involved the loss of the bend structure of this region, while the N-terminus turn was maintained. Numerous studies have shown that polyphenolic molecules can act upon various biological targets, and the formation of this type of complex might be one of the possible modes of action.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anthocyanins / chemistry
  • Binding Sites
  • Bradykinin / chemistry*
  • Dimerization
  • Flavonoids / chemistry*
  • Magnetic Resonance Spectroscopy
  • Models, Molecular
  • Peptides / chemistry
  • Phenols / chemistry*
  • Polyphenols
  • Protein Folding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Temperature

Substances

  • Anthocyanins
  • Flavonoids
  • Peptides
  • Phenols
  • Polyphenols
  • proanthocyanidin B3
  • Bradykinin