The Binding of Oligopeptides to Cyclodextrins: The Role of the Tyrosine Group.
Abstract
The formation of alpha-cyclodextrin (alpha-CD) and beta-cyclodextrin (beta-CD) inclusion complexes with free tyrosine and the tyrosine residues in two oligopeptides were investigated using steady-state fluorescence spectroscopy. The oligopeptides consist of five amino acids (pentapeptide) and the tyrosine residues are at the n-terminus of both peptides. The two peptides used in this study have specific biological applications and are known to bind selectively to specific 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 effect on alpha-CD binding. However, tyrosine binding to beta-CD was dependent on the size (free tyrosine vs. peptide), structure, and pentapeptide conformation.
Document Details
- Document Type
- Technical Report
- Publication Date
- Aug 01, 1996
- Accession Number
- ADA313397
Entities
People
- E. J. Bekos
- F. V. Bright
- J. A. Gardella Jr.
Organizations
- University at Buffalo