Conformational stability of a type II' β-turn motif in human growth hormone [6-13] peptide analogues at hydrophobic surfaces

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The interactive properties of several peptides related to human growth hormone (hGH) [6-13] containing a type II' β-turn motif have been investigated using reversed-phase high-performance liquid chromatography (RP- HPLC). Various chromatographic parameters related to the hydrophobic interactive surface area and binding affinity were measured over the range of temperatures between 5 and 85 C. Variations in these parameters were consistent with significant differences in the relative stability of the type II' β-turn structures of these peptidomimetics. The effect of changes in peptide conformation were also investigated through the analysis of band- broadening behaviour during the chromatographic process. Significant variations in bandwidth observed at discrete temperatures were related to the rate of interconversion between the type II' β-turn and more extended conformers. These investigations further document the potential of RP-HPLC for monitoring subtle changes in peptide secondary structure at hydrophobic interfaces.

Original languageEnglish
Pages (from-to)394-403
Number of pages10
JournalJournal of Peptide Research
Issue number5
Publication statusPublished - 15 Jul 1997


  • β-turn
  • Binding affinity
  • Contact surface area
  • Human growth hormone
  • Hypoglycaemic activity
  • Peptidomimetics
  • Reversed phase HPLC

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