Chromatographic and fluorometric study of interactions between thiophilic and hydrophobic ligands and tryptophan peptide homologues

• Published in: Journal of Chromatography A Vol. 1107; no. 1; pp. 46 - 51
• Main Authors: Xue, Bo, Ersson, Bo, Porath, Jerker, Caldwell, Karin
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 24.02.2006; Elsevier
• Subjects: Analytical chemistry; Chemistry; Chromatographic methods and physical methods associated with chromatography; Chromatography; Chromatography, Liquid - methods; Exact sciences and technology; Fluorescence; Hydrogen-Ion Concentration; Hydrophobic interaction; Ligands; Other chromatographic methods; Peptides - chemistry; Peptides - metabolism; Salts; Spectrometry, Fluorescence - methods; Spectrophotometry, Ultraviolet; Temperature; Thiophilic adsorption; Tryptophan; Tryptophan - metabolism; Fluorescence; Tryptophan; Hydrophobic interaction; Thiophilic adsorption; Chromatography; Fluorescence: Tryptophan: Hydrophobic interaction; Gibbs free energy; Adsorption energy; Peptides; Enthalpy; Tripeptide; Temperature effect; Retention factor; Entropy; Mobile phase; Fluorescence spectrometry; Operating conditions; α-Aminoacid; Salt effect; Affinity chromatography; Hydrophobic chromatography; Concentration effect; Dipeptides; pH; Thiophilic adsorption: Chromatography; Thermodynamic properties
• ISSN: 0021-9673
• DOI: 10.1016/j.chroma.2005.11.040

The interactions of tryptophan and its peptide homologues with thiophilic ligands were studied in terms of their chromatographic retention and steady-state fluorescence under various conditions, and compared with non-polar structures typically regarded as pure hydrophobic ligands. The experimental results show that both non-polar and polar interactions are involved in what has been termed “thiophilic adsorption chromatography”.