Abstract
The dynamics of several peptides in reversed-phase high-performance liquid chromatography (RP-HPLC) have been investigated on both n-octadecyl (C18) silica and n-butyl (C4) silica sorbents. In particular, the conformational interconversions and the relative rates of chromatographic relaxation of bombesin, glucagon, and β-endorphin on both C18 and C4 n-alkylsilicas were monitored by examining changes in the experimental bandwidths of these peptides as a function of temperature and column residence time under linear gradient elution RP-HPLC conditions. The observed band-broadening trends were correlated with previously derived retention parameters and thermodynamic descriptors of the association process determined for bombesin, β-endorphin, glucagon, and a control peptide, penta-l-phenylalanine. This study confirms that bandwidth measurements can be used as an integral experimental component to study the effect of the secondary structure of peptidic solutes on their RP-HPLC retention behavior. Further, the data demonstrate the utility of RP-HPLC as a tool to examine peptide conformational dynamics at hydrophobic surfaces. The relevance of these results to the general phenomenon of peptide-lipid interactions is discussed in terms of the associated evidence for lipid-induced changes in the conformation of these three bioactive peptides.
| Original language | English |
|---|---|
| Pages (from-to) | 3038-3047 |
| Number of pages | 10 |
| Journal | Analytical Chemistry |
| Volume | 65 |
| Issue number | 21 |
| DOIs | |
| Publication status | Published - 1 Nov 1993 |
Cite this
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High-Performance Liquid Chromatography of Amino Acids, Peptides, and Proteins. 123. Dynamics of Peptides in Reversed-Phase High-Performance Liquid Chromatography. / Purcell, Anthony W.; Aguilar, Marie Isabel; Hearn, Milton.
In: Analytical Chemistry, Vol. 65, No. 21, 01.11.1993, p. 3038-3047.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - High-Performance Liquid Chromatography of Amino Acids, Peptides, and Proteins. 123. Dynamics of Peptides in Reversed-Phase High-Performance Liquid Chromatography
AU - Purcell, Anthony W.
AU - Aguilar, Marie Isabel
AU - Hearn, Milton
PY - 1993/11/1
Y1 - 1993/11/1
N2 - The dynamics of several peptides in reversed-phase high-performance liquid chromatography (RP-HPLC) have been investigated on both n-octadecyl (C18) silica and n-butyl (C4) silica sorbents. In particular, the conformational interconversions and the relative rates of chromatographic relaxation of bombesin, glucagon, and β-endorphin on both C18 and C4 n-alkylsilicas were monitored by examining changes in the experimental bandwidths of these peptides as a function of temperature and column residence time under linear gradient elution RP-HPLC conditions. The observed band-broadening trends were correlated with previously derived retention parameters and thermodynamic descriptors of the association process determined for bombesin, β-endorphin, glucagon, and a control peptide, penta-l-phenylalanine. This study confirms that bandwidth measurements can be used as an integral experimental component to study the effect of the secondary structure of peptidic solutes on their RP-HPLC retention behavior. Further, the data demonstrate the utility of RP-HPLC as a tool to examine peptide conformational dynamics at hydrophobic surfaces. The relevance of these results to the general phenomenon of peptide-lipid interactions is discussed in terms of the associated evidence for lipid-induced changes in the conformation of these three bioactive peptides.
AB - The dynamics of several peptides in reversed-phase high-performance liquid chromatography (RP-HPLC) have been investigated on both n-octadecyl (C18) silica and n-butyl (C4) silica sorbents. In particular, the conformational interconversions and the relative rates of chromatographic relaxation of bombesin, glucagon, and β-endorphin on both C18 and C4 n-alkylsilicas were monitored by examining changes in the experimental bandwidths of these peptides as a function of temperature and column residence time under linear gradient elution RP-HPLC conditions. The observed band-broadening trends were correlated with previously derived retention parameters and thermodynamic descriptors of the association process determined for bombesin, β-endorphin, glucagon, and a control peptide, penta-l-phenylalanine. This study confirms that bandwidth measurements can be used as an integral experimental component to study the effect of the secondary structure of peptidic solutes on their RP-HPLC retention behavior. Further, the data demonstrate the utility of RP-HPLC as a tool to examine peptide conformational dynamics at hydrophobic surfaces. The relevance of these results to the general phenomenon of peptide-lipid interactions is discussed in terms of the associated evidence for lipid-induced changes in the conformation of these three bioactive peptides.
UR - http://www.scopus.com/inward/record.url?scp=0027703760&partnerID=8YFLogxK
U2 - 10.1021/ac00069a016
DO - 10.1021/ac00069a016
M3 - Article
VL - 65
SP - 3038
EP - 3047
JO - Analytical Chemistry
JF - Analytical Chemistry
SN - 0003-2700
IS - 21
ER -