Design and chemical synthesis of a 32 residues chimeric microprotein inhibiting both trypsin and carboxypeptidase A.
A chimeric peptide, 32 amino acids long, bearing two active sites, one inhibiting trypsin (Kd = 1.8 10(-9) M), one carboxypeptidase A (Kd = 3 10(-9) M), was designed and synthesized. It is a "squash inhibitor" (EETI II, 28 amino acids) elongated with the 4 amino acids from the C-terminus of the potato carboxypeptidase inhibitor. It has 3 disulfide bridges assembled in the particular knotted topology shared by the two inhibitors, by conotoxin omega, and possibly by E. coli enterotoxin ST1b.
Le-Nguyen
D
D
Centre CNRS-INSERM de Pharmacologie-Endocrinologie, Montpellier, France.
Mattras
H
H
Coletti-Previero
M A
MA
Castro
B
B
D000595:Amino Acid Sequence; D002268:Carboxypeptidases / Q000037:antagonists & inhibitors*; D043422:Carboxypeptidases A; D003545:Cysteine; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000138:chemical synthesis*; D011506:Proteins / Q000138:chemical synthesis; D014357:Trypsin / Q000378:metabolism; D014361:Trypsin Inhibitors / Q000378:metabolism
D046911:Macromolecular Substances; D011480:Protease Inhibitors; D011506:Proteins; D014361:Trypsin Inhibitors; D002268:Carboxypeptidases; D043422:Carboxypeptidases A; D014357:Trypsin; D003545:Cysteine