Development of Synthetic Catalysts for Peptide Bond Cleavage Synthesis and Complete Kinetic Analysis of Compounds 6A, 7A, 8A
Abstract
Synthetic mimics for carboxypeptidase A will be synthesized and the structural and chemical factors responsible for catalytic peptidase activity will be probed. Ditopic macrocyclic receptors have been designed which incorporate the salient features of the enzyme analog, namely high affinity complex formation, general base and general acid catalysis, and covalent catalysis. Once synthesized the resulting macrocycle-metal ion complexes should non-specifically promote the hydrolysis of C-terminal peptide bonds. The initial macrocycles will have several types of coordination sites: nitrogen-containing heterocycles, ammonium and ether oxygens. One side of the ditopic receptor will preferentially bind zinc(II) ion, the other peptide substrate. Keywords: Enzyme mimics, Supramolecular, Carboxypeptidase A, Polyammonium macrocycles, Synthetic catalysts, Peptide bond cleavage, Kinetic analysis, Ring systems.
Document Details
- Document Type
- Technical Report
- Publication Date
- May 15, 1990
- Accession Number
- ADA222703
Entities
People
- Kristin Mertes
- P. I. Bowman
Organizations
- University of Kansas