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• W2084920886 endingPage "221" @default.
• W2084920886 startingPage "205" @default.
• W2084920886 abstract "The reversed-phase retention behaviour of two series of peptides, one non-helical and the other α-helical, was studied under various linear AB gradients in order to determine the effect of peptide conformation on selectivity of the separation. The non-helical series, designated X1, with the sequence Ac-XLGAKGAGVG-amide, exhibited negligible α-helical content in a hydrophobic medium; whereas, the amphipathic α-helical series, designated AX9, with the sequence Ac-EAEKAAKEXEKAAKEAEK-amide, exhibited high α-helical content in a hydrophobic medium. We have shown that plots of log k vs. φ (where k is the median capacity factor and φ is the median volume fraction of organic solvent) are very similar for any one peptide conformation, i.e., peptides from either the non-helical or amphipathic α-helical series exhibit similar S (solute parameter) values and the b (gradient steepness parameter) values are also similar for 17 different amino acid substitutions within each series of peptides. If mixtures of peptides from the two different series are separated using either increasing or decreasing gradient rates, large increases in resolution occur due to selectivity, which may be attributed to the difference in the log k vs. φ plots for each series of peptides. In addition, by using a polymer of an X1 peptide, which is 20 residues in length, it has been shown that the molecular mass difference between the X1 and the AX9 series of peptides is not sufficient to account for the selectivity difference. The S value of a non-amphipathic α-helical peptide further suggested that the difference in selectivity between the two series of peptides was due to differences in conformation. We believe that the peptide mixtures presented here providea a good model for studyingselectivity effects due to conformational differences between peptides, an important concern when attempting to develop rational approaches to the prediction and optimization of peptide separation protocols from primary sequence information alone." @default.
• W2084920886 created "2016-06-24" @default.
• W2084920886 creator A5046150106 @default.
• W2084920886 creator A5052295449 @default.
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• W2084920886 date "1995-03-01" @default.
• W2084920886 modified "2023-10-10" @default.
• W2084920886 title "Selectivity due to conformational differences between helical and non-helical peptides in reversed-phase chromatography" @default.
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• W2084920886 doi "https://doi.org/10.1016/0021-9673(94)01147-7" @default.
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