Induction of amphipathic helical peptide structures in RP-HPLC.

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Abstract

The retention behavior of a series of amphipathic peptide multimers based on the amino acid sequence [KSEEQLA]n has been investigated using reversed-phase high performance liquid chromatography (RP-HPLC). Structure-retention parameters which are related to the hydrophobic contact area and affinity of these peptides for the immobilized hydrocarbonaceous ligands were determined over a range of operating temperatures between 5 degrees and 85 degrees C. The influence of ligand hydrophobicity was assessed by comparison of peptide retention behavior using an n-octadecyl (C18)- and an n-butyl (C4)-silica of similar ligand density. The results demonstrated that ligand-mediated conformational effects can stabilize peptide structure depending on the chromatographic residence time and peptide length. In particular, more highly stabilized secondary structures were evident for the longer peptides. In addition, the amphipathic secondary structure of the peptides were more effectively stabilized by the more hydrophobic C18 ligands relative to the shorter C4 ligands. Additional information on the interactive dynamics of these peptide multimers was obtained from analysis of bandwidth dependencies under the different chromatographic conditions. These studies provide further insight into the role which hydrophobic forces can play in the stabilization of peptide structures.

Original languageEnglish
Pages (from-to)160-170
Number of pages11
JournalPeptide Research
Volume8
Issue number3
Publication statusPublished - 1 Jan 1995

Cite this

@article{de1f1eb32ff94f9ba381d7c28b0c51cc,
title = "Induction of amphipathic helical peptide structures in RP-HPLC.",
abstract = "The retention behavior of a series of amphipathic peptide multimers based on the amino acid sequence [KSEEQLA]n has been investigated using reversed-phase high performance liquid chromatography (RP-HPLC). Structure-retention parameters which are related to the hydrophobic contact area and affinity of these peptides for the immobilized hydrocarbonaceous ligands were determined over a range of operating temperatures between 5 degrees and 85 degrees C. The influence of ligand hydrophobicity was assessed by comparison of peptide retention behavior using an n-octadecyl (C18)- and an n-butyl (C4)-silica of similar ligand density. The results demonstrated that ligand-mediated conformational effects can stabilize peptide structure depending on the chromatographic residence time and peptide length. In particular, more highly stabilized secondary structures were evident for the longer peptides. In addition, the amphipathic secondary structure of the peptides were more effectively stabilized by the more hydrophobic C18 ligands relative to the shorter C4 ligands. Additional information on the interactive dynamics of these peptide multimers was obtained from analysis of bandwidth dependencies under the different chromatographic conditions. These studies provide further insight into the role which hydrophobic forces can play in the stabilization of peptide structures.",
author = "Purcell, {A. W.} and Aguilar, {M. I.} and Wettenhall, {R. E.} and Hearn, {M. T.}",
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Induction of amphipathic helical peptide structures in RP-HPLC. / Purcell, A. W.; Aguilar, M. I.; Wettenhall, R. E.; Hearn, M. T.

In: Peptide Research, Vol. 8, No. 3, 01.01.1995, p. 160-170.

Research output: Contribution to journalArticleResearchpeer-review

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T1 - Induction of amphipathic helical peptide structures in RP-HPLC.

AU - Purcell, A. W.

AU - Aguilar, M. I.

AU - Wettenhall, R. E.

AU - Hearn, M. T.

PY - 1995/1/1

Y1 - 1995/1/1

N2 - The retention behavior of a series of amphipathic peptide multimers based on the amino acid sequence [KSEEQLA]n has been investigated using reversed-phase high performance liquid chromatography (RP-HPLC). Structure-retention parameters which are related to the hydrophobic contact area and affinity of these peptides for the immobilized hydrocarbonaceous ligands were determined over a range of operating temperatures between 5 degrees and 85 degrees C. The influence of ligand hydrophobicity was assessed by comparison of peptide retention behavior using an n-octadecyl (C18)- and an n-butyl (C4)-silica of similar ligand density. The results demonstrated that ligand-mediated conformational effects can stabilize peptide structure depending on the chromatographic residence time and peptide length. In particular, more highly stabilized secondary structures were evident for the longer peptides. In addition, the amphipathic secondary structure of the peptides were more effectively stabilized by the more hydrophobic C18 ligands relative to the shorter C4 ligands. Additional information on the interactive dynamics of these peptide multimers was obtained from analysis of bandwidth dependencies under the different chromatographic conditions. These studies provide further insight into the role which hydrophobic forces can play in the stabilization of peptide structures.

AB - The retention behavior of a series of amphipathic peptide multimers based on the amino acid sequence [KSEEQLA]n has been investigated using reversed-phase high performance liquid chromatography (RP-HPLC). Structure-retention parameters which are related to the hydrophobic contact area and affinity of these peptides for the immobilized hydrocarbonaceous ligands were determined over a range of operating temperatures between 5 degrees and 85 degrees C. The influence of ligand hydrophobicity was assessed by comparison of peptide retention behavior using an n-octadecyl (C18)- and an n-butyl (C4)-silica of similar ligand density. The results demonstrated that ligand-mediated conformational effects can stabilize peptide structure depending on the chromatographic residence time and peptide length. In particular, more highly stabilized secondary structures were evident for the longer peptides. In addition, the amphipathic secondary structure of the peptides were more effectively stabilized by the more hydrophobic C18 ligands relative to the shorter C4 ligands. Additional information on the interactive dynamics of these peptide multimers was obtained from analysis of bandwidth dependencies under the different chromatographic conditions. These studies provide further insight into the role which hydrophobic forces can play in the stabilization of peptide structures.

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