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The binding of free oligopeptides to cyclodextrins: The role of the tyrosine group

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Abstract

The formation ofα-cyclodextrin (α-CD) and,β-cyclodextrin (β-CD) inclusion complexes with free tyrosine and the tyrosine residues within two free oligopeptides were investigated using steady-state fluorescence spectroscopy. The oligopeptides consist of five amino acids (pentapeptide) and the tyrosine residues are located at then-termini. The two peptides used in this study have well-known biological functions and are known to bind selectively to specific cell receptors. Cyclodextrins were used to model this receptor-peptide (protein-ligand) interaction. Equilibrium binding constants and the enthalpy and entropy of binding were recovered. Molecular size of the tyrosine-containing species and pH (7.0 vs. 10.0) were found to have little affect onα-CD binding. However, tyrosine binding toβ-CD was dependent on the size (free tyrosine vs. peptide), structure, and pentapeptide conformation.

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Bekos, E.J., Gardella, J.A. & Bright, F.V. The binding of free oligopeptides to cyclodextrins: The role of the tyrosine group. J Incl Phenom Macrocycl Chem 26, 185–195 (1996). https://doi.org/10.1007/BF01053537

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