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- W2996413261 abstract "Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins The interaction of a range of cyclodextrins with amino acids, both free and in proteins has been investigated using sensitive microcalorimetry and spectroscopic techniques. With a view towards possible applications in chiral separation technologies, isothermal titration calorimetry (ITC) was used to study the complexation of cyclodextrins with the enantiomers of ?-amino acids by competition with p-nitrophenolate or p-aminobenzoic acid under various pH conditions. It was found the majority of amino acids showed no complexation. However, complexes of alpha-cyclodextrin with phenylalanine, and tryptophan demonstrated small, but distinct, differences in dissociation constants for their separate enantiomers. Thermodynamic parameters (Kd, DeltaH" @default.
- W2996413261 created "2019-12-26" @default.
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- W2996413261 date "1997-01-01" @default.
- W2996413261 modified "2023-09-23" @default.
- W2996413261 title "Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins" @default.
- W2996413261 hasPublicationYear "1997" @default.
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