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Reference type: Journal
Authors: Kim H, Guiochon G
Article Title: Adsorption on molecularly imprinted polymers of structural analogues of a template. single-component adsorption isotherm data.
Publication date: 2005
Journal: Analytical Chemistry
Volume: 77
Issue: (19)
Page numbers: 6415-6425.
DOI: 10.1021/ac050914+

Abstract: The equilibrium adsorption isotherms on two otherwise identical polymers, one imprinted with Fmoc-L-tryptophan (Fmoc-(L)-Trp) (MIP), the other nonimprinted (NIP), of compounds that are structural analogues of the template were acquired by frontal analysis (FA) in an acetonitrile/ acetic acid (99/1 v/v) mobile phase, over a wide concentration range (from 0.005 to 50 mM). These analogues were Fmoc-L-tyrosine, Fmoc-L-serine, Fmoc-(L)-phenyalanine, Fmoc-glycine (Fmoc-Gly), Finoc-(L)-tryptophan pentafluorophenyl ester (Fmoc-L-Trp(OPfp)), and their antipodes. These substrates have different numbers of functional groups able to interact with the 4-vinylpyridine groups of the polymer. For a given number of the functional groups, these substrates have different hydro-phobicities of their side groups (as indicated by their partition coefficients (log Pow) in the octanol-water system (e.g., from 4.74 for Fmoc-Trp to 2.53 for Fmoc-Gly)). Statistical results from the fitting of the FA data to Langmuirian isotherm models, the calculation of the affinity energy distribution, and the comparison of calculated and experimental band profiles show that all these sets of FA data are best accounted. for by a tri-Langmuir isotherm model, except for the data of Fmoc-L-Trp(0Pfp) that are best modeled by a simple Langmuir isotherm. So, all compounds but Fmoc-L-Trp(0Pfp) find three different types of adsorption sites on both the MIP and the NIP. The properties of these different types of sites were studied systematically. The results show that the affinity of the structural analogues for the NIP is controlled mostly by the number of the functional groups on the substrates and somewhat by the hydrophobicity of their side groups. These two factors control also the MIP affinity toward the enantiomers of the structural analogues that have a stereochemistry different from that of the template. In contrast, the affinity of the highest affinity sites of the MIP toward the enantiomers of these structural analogues that have the same stereochemistry as the template is highest for the imprinted molecule (Fmoc-L-Trp). The separation of the template from the substrates with the same stereochemistry is influenced by the number of the functional groups on the substrates that can interact with the highest affinity sites on the MIP. The separation of the enantiomers of the analogues of the substrates was also achieved on the MIP, and these enantiomeric separations are influenced by the hydrophobicity of the substrates
Template and target information: Fmoc-L-tryptophan, Fmoc-(L)-Trp

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