Abstract
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 language | English |
|---|---|
| Pages (from-to) | 394-403 |
| Number of pages | 10 |
| Journal | Journal of Peptide Research |
| Volume | 49 |
| Issue number | 5 |
| Publication status | Published - 15 Jul 1997 |
Keywords
- β-turn
- Binding affinity
- Contact surface area
- Human growth hormone
- Hypoglycaemic activity
- Peptidomimetics
- Reversed phase HPLC