Accession Number : ADA183251
Title : Development of Synthetic Catalysts for Peptide Bond Cleavage (Synthesis and Complete Kinetic Analysis of Compounds 6A, 7A, 8A).
Descriptive Note : Annual rept. 6 Aug 86-5 Aug 87,
Corporate Author : KANSAS UNIV LAWRENCE
Personal Author(s) : Mertes,Kristin B ; Mertes,Mathias P
PDF Url : ADA183251
Report Date : 05 Aug 1987
Pagination or Media Count : 10
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, ammonium and ether oxygens. One side of ditopic receptor will preferentially bind zinc (II) ion, the other the peptide substrate.
Descriptors : *CATALYSTS, *PEPTIDE HYDROLASES, *SYNTHESIS(CHEMISTRY), ACIDS, KINETICS, PEPTIDES, SUBSTRATES, SYNTHESIS, COVALENT BONDS, ANALOG SYSTEMS, ENZYMES, HYDROLYSIS, BONDING, CLEAVAGE, CHEMICAL PROPERTIES, ZINC, MOLECULAR STRUCTURE, AMMONIUM COMPOUNDS, OXYGEN, NITROGEN HETEROCYCLIC COMPOUNDS
Subject Categories : Biochemistry
Distribution Statement : APPROVED FOR PUBLIC RELEASE