High-performance liquid chromatography of amino acids, peptides and proteins CXV. Thermodynamic behaviour of peptides in reversed-phase chromatography

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Abstract

The thermodynamic behaviour of three peptides, bombesin, β-endorphin and glucagon, was studied under reversed-phase high-performance liquid chromatographic conditions. Experimental data related to the interactive surface contact area (S values) and solute affinity (log k0) were derived over a range of temperatures between 5 and 85°C. These experimental conditions allowed changes in the secondary structure of the solute to be monitored. The influence of the nature of the stationary phase ligand on the relative conformational stability of the three peptides was analysed by acquiring data with n-octadecyl silica (C18) and n-butyl silica (C4) sorbents. Values for the relative changes in entropy and ethalpy associated with the interactive process were also determined. The results provide further insight into the factors involved with the stabilization of secondary structure and the mechanism of the interaction of peptides with hydrophobic surfaces.

Original languageEnglish
Pages (from-to)103-117
Number of pages15
JournalJournal of Chromatography A
Volume593
Issue number1-2
DOIs
Publication statusPublished - 28 Feb 1992

Cite this

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title = "High-performance liquid chromatography of amino acids, peptides and proteins CXV. Thermodynamic behaviour of peptides in reversed-phase chromatography",
abstract = "The thermodynamic behaviour of three peptides, bombesin, β-endorphin and glucagon, was studied under reversed-phase high-performance liquid chromatographic conditions. Experimental data related to the interactive surface contact area (S values) and solute affinity (log k0) were derived over a range of temperatures between 5 and 85°C. These experimental conditions allowed changes in the secondary structure of the solute to be monitored. The influence of the nature of the stationary phase ligand on the relative conformational stability of the three peptides was analysed by acquiring data with n-octadecyl silica (C18) and n-butyl silica (C4) sorbents. Values for the relative changes in entropy and ethalpy associated with the interactive process were also determined. The results provide further insight into the factors involved with the stabilization of secondary structure and the mechanism of the interaction of peptides with hydrophobic surfaces.",
author = "Purcell, {A. W.} and Aguilar, {M. I.} and Hearn, {M. T W}",
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T1 - High-performance liquid chromatography of amino acids, peptides and proteins CXV. Thermodynamic behaviour of peptides in reversed-phase chromatography

AU - Purcell, A. W.

AU - Aguilar, M. I.

AU - Hearn, M. T W

PY - 1992/2/28

Y1 - 1992/2/28

N2 - The thermodynamic behaviour of three peptides, bombesin, β-endorphin and glucagon, was studied under reversed-phase high-performance liquid chromatographic conditions. Experimental data related to the interactive surface contact area (S values) and solute affinity (log k0) were derived over a range of temperatures between 5 and 85°C. These experimental conditions allowed changes in the secondary structure of the solute to be monitored. The influence of the nature of the stationary phase ligand on the relative conformational stability of the three peptides was analysed by acquiring data with n-octadecyl silica (C18) and n-butyl silica (C4) sorbents. Values for the relative changes in entropy and ethalpy associated with the interactive process were also determined. The results provide further insight into the factors involved with the stabilization of secondary structure and the mechanism of the interaction of peptides with hydrophobic surfaces.

AB - The thermodynamic behaviour of three peptides, bombesin, β-endorphin and glucagon, was studied under reversed-phase high-performance liquid chromatographic conditions. Experimental data related to the interactive surface contact area (S values) and solute affinity (log k0) were derived over a range of temperatures between 5 and 85°C. These experimental conditions allowed changes in the secondary structure of the solute to be monitored. The influence of the nature of the stationary phase ligand on the relative conformational stability of the three peptides was analysed by acquiring data with n-octadecyl silica (C18) and n-butyl silica (C4) sorbents. Values for the relative changes in entropy and ethalpy associated with the interactive process were also determined. The results provide further insight into the factors involved with the stabilization of secondary structure and the mechanism of the interaction of peptides with hydrophobic surfaces.

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DO - 10.1016/0021-9673(92)80274-X

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