Slow tert-butyl ester acidolysis and peptide 3(10)-helix to alpha-helix transition in HFIP solution

Biopolymers. 2007;88(2):233-8. doi: 10.1002/bip.20680.

Abstract

We have already shown by CD and NMR techniques that the terminally protected homo-octapeptides Z (and Ac)-[L-(alphaMe)Val](8)-OtBu undergo a slow and irreversible 3(10)-helix to alpha-helix transition when dissolved in 1,1,1,3,3,3-hexafluoroisopropanol. In the present work, we find by HPLC and CD that under the aforementioned experimental conditions, a slow acidolysis of the tert-butyl ester functionality does take place affording the corresponding octapeptide free acids. The results of our combined chromatographic and spectroscopic experiments are confirmed by a comparison with the properties of independently synthesized and chemically characterized authentic compounds.

MeSH terms

  • Chromatography, High Pressure Liquid
  • Circular Dichroism
  • Esters / chemistry
  • Magnetic Resonance Spectroscopy
  • Peptides / chemistry*
  • Propanols
  • Protein Structure, Secondary
  • Solutions
  • Spectroscopy, Fourier Transform Infrared

Substances

  • Esters
  • Peptides
  • Propanols
  • Solutions
  • hexafluoroisopropanol