Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins

[摘要] 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

[发布机构] University:University of Glasgow

[关键词] Biochemistry