Miniature Organic Model of Chymotrypsin: Synthesis and Evaluation.
Abstract
Three artificial enzymes (benzymes), based on alpha, beta and gamma-cyclodextrins (cycloamyloses) were synthesized by attaching the three catalytic groups of chymotrypsin; 1) hydroxyl group 2) imidazolyl group and 3) carboxylate ion to known binders, cyclodextrins. These molecules have both a catalytic portion and a binding portion in them and thus they can serve as complete, albeit artificial enzymes. Beta-Benzyme has approximately the same catalytic activity as the real enzyme although the molecular weight of the artificial enzyme (1365) is 1/18 the molecular weight of the real enzyme (24,800). Results indicate that both the artificial chymotrypsin and the real chymotrypsin have similar mechanisms. The artificial enzyme shows increased activity at high pH and temperature conditions whereas the real enzyme denatures at relatively milder pH and thermal conditions. The artificial enzymes show a specificity based on the size of the cyclodextrin cavity. Five publications, one patent and three major presentations have resulted from this study. Synthetic, mechanistic and specificity investigations of these enzymes are planned for the second year.
Document Details
- Document Type
- Technical Report
- Publication Date
- Mar 23, 1987
- Accession Number
- ADA178987
Entities
People
- Myron L. Bender
Organizations
- Northwestern University