Active site chemical mutagenesis of Ecballium elaterium trypsin inhibitor II: new microproteins inhibiting elastase and chymotrypsin.
Seven microproteins analogous to Ecballium elaterium Trypsin Inhibitor II. were synthesized. The study of their inhibiting power showed a change in selectivity from trypsin to elastase for 5 of the compounds and to alpha-chymotrypsin for another one. A striking characteristic that appeared during this synthetic approach was the ability of the 28 amino acid peptides to refold and close correctly the 3 disulfide bridges, giving in each case an active compound.
Favel
A
A
Centre CNRS-INSERM de Pharmacologie-Endocrinologie, Montpellier, France.
Le-Nguyen
D
D
Coletti-Previero
M A
MA
Castro
B
B
D000595:Amino Acid Sequence; D001665:Binding Sites; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D004220:Disulfides; D007930:Leucine; D008715:Methionine; D008969:Molecular Sequence Data; D009153:Mutagens; D009154:Mutation; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D010940:Plant Proteins / Q000138:chemical synthesis / Q000235:genetics* / Q000494:pharmacology; D014361:Trypsin Inhibitors / Q000138:chemical synthesis / Q000235:genetics* / Q000494:pharmacology
D004220:Disulfides; D009153:Mutagens; D010940:Plant Proteins; D014361:Trypsin Inhibitors; D008715:Methionine; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D007930:Leucine