Accession Number:

ADA222703

Title:

Development of Synthetic Catalysts for Peptide Bond Cleavage Synthesis and Complete Kinetic Analysis of Compounds 6A, 7A, 8A

Descriptive Note:

Final rept.

Corporate Author:

KANSAS UNIV LAWRENCE

Personal Author(s):

Report Date:

1990-05-15

Pagination or Media Count:

10.0

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 zincII ion, the other peptide substrate. Keywords Enzyme mimics, Supramolecular, Carboxypeptidase A, Polyammonium macrocycles, Synthetic catalysts, Peptide bond cleavage, Kinetic analysis, Ring systems.

Subject Categories:

  • Biochemistry

Distribution Statement:

APPROVED FOR PUBLIC RELEASE