Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins

Lovatt, Michelle (1997) Microcalorimetry of Cyclodextrin Interactions with Amino Acids and Proteins. PhD thesis, University of Glasgow.

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

• Item Type: Thesis (PhD)
• Qualification Level: Doctoral
• Additional Information: Adviser: Alan Cooper
• Keywords: Biochemistry
• Date of Award: 1997
• Depositing User: Enlighten Team
• Unique ID: glathesis:1997-74847
• Copyright: Copyright of this thesis is held by the author.
• Date Deposited: 27 Sep 2019 15:52
• Last Modified: 27 Sep 2019 15:52
• URI: https://theses.gla.ac.uk/id/eprint/74847