Chemical synthesis of new trypsin, chymotrypsin and elastase inhibitors by amino-acid substitutions in a trypsin inhibitor from squash seeds (CMTI III).
Five new analogues of squash trypsin inhibitor CMTI III were obtained by the solid-phase method, exhibiting antitrypsin, antichymotrypsin or antielastase activity. Modification in the reactive site region changes dramatically the specificity, whereas substitution in non-contact positions facilitates the refolding of the reduced form of the peptides and does not have a significant influence on the association equilibrium constants of the inhibitor analogues with cognate enzymes.
Rolka
K
K
Institute of Chemistry, University of Gdańsk, Poland.
Kupryszewski
G
G
Ragnarsson
U
U
Otlewski
J
J
Krokoszynska
I
I
Wilusz
T
T
D000595:Amino Acid Sequence; D002918:Chymotrypsin / Q000037:antagonists & inhibitors*; D006801:Humans; D007962:Leukocytes / Q000201:enzymology; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D012639:Seeds / Q000032:analysis*; D013379:Substrate Specificity; D014361:Trypsin Inhibitors / Q000138:chemical synthesis* / Q000494:pharmacology; D014961:X-Ray Diffraction
D014361:Trypsin Inhibitors; D002918:Chymotrypsin; D010196:Pancreatic Elastase