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.
D000595:Amino Acid Sequence; D007611:Aprotinin / Q000138:chemical synthesis* / Q000494:pharmacology; D011485:Protein Binding; D011487:Protein Conformation; D013329:Structure-Activity Relationship
D007611:Aprotinin