Endothelin 1: conformation and aggregation

Pept Res. 1992 Mar-Apr;5(2):97-101.

Abstract

The features of the far UV CD spectrum of endothelin 1 (ET 1) in water-containing solutions rules out the presence of any alpha-helical contribution, thus questioning the conclusions made by several authors on the basis of NMR investigations. We propose here a structural model, based on a succession of beta turns, which is consistent with both the NMR and the CD data. Using electron microscopy, we show that ET 1 can form "micelles," and the micelles self-associate into percolation clusters which have a fractal dimension of 1.23 in a 2D space. These data, too, are in agreement with our proposed structural model.

MeSH terms

  • Amino Acid Sequence
  • Circular Dichroism
  • Endothelins / chemistry*
  • Microscopy, Electron
  • Models, Structural
  • Molecular Sequence Data
  • Protein Conformation
  • Solutions

Substances

  • Endothelins
  • Solutions