Conformational stability of a type II' beta-turn motif in human growth hormone [6-13] peptide analogues at hydrophobic surfaces.
The interactive properties of several peptides related to human growth hormone (hGH) [6-13] containing a type II' beta-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 degrees C. Variations in these parameters were consistent with significant differences in the relative stability of the type II' beta-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' beta-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.
Lee
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TH
Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia.
Thompson
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PE
Hearn
M T
MT
Aguilar
M I
MI
D002851:Chromatography, High Pressure Liquid; D013006:Growth Hormone / Q000737:chemistry*; D019382:Human Growth Hormone / Q000031:analogs & derivatives* / Q000737:chemistry*; D006801:Humans; D008961:Models, Structural; D010446:Peptide Fragments / Q000737:chemistry*; D017433:Protein Structure, Secondary; D013816:Thermodynamics
D010446:Peptide Fragments; D019382:Human Growth Hormone; C037849:somatotropin (6-13); D013006:Growth Hormone