Ernst Truscheit

Semisynthetic engineering of proteinase inhibitor homologues.

A semisynthetic approach to modulate the inhibitory specificity of aprotinin, the Kunitz trypsin inhibitor from bovine mast cells, is described. By the use of peptide-chemical procedures a single amino acid of its reactive site can be replaced by any other coded or non-coded amino acid. Thus, a series of aprotinin homologues have been prepared which demonstrate the individual contribution of a single side chain to the inhibition of a particular target proteinase and enable specific inhibitors to be designed.

Drug concentration monitoring, microbial alpha-glucosidase inhibitors, plasminogen activators

Drug Concentration Monitoring.- Microbial Alpha-Glucosidase Inhibitors: Chemistry, Biochemistry and Therapeutic Potential.- Plasminogen Activators: Molecular Properties, Biological Cell Function and Clinical Application.- Author Index Volumes 1-7.