title: Chemical synthesis of new trypsin, chymotrypsin and elastase inhibitors by amino-acid substitutions in a trypsin inhibitor from squash seeds (CMTI III).
abstract: 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.
authors.affiliation: Institute of Chemistry, University of Gdańsk, Poland.
authors.forename: K
authors.initials: K
authors.lastname: Rolka
authors.forename: G
authors.initials: G
authors.lastname: Kupryszewski
authors.forename: U
authors.initials: U
authors.lastname: Ragnarsson
authors.forename: J
authors.initials: J
authors.lastname: Otlewski
authors.forename: I
authors.initials: I
authors.lastname: Krokoszynska
authors.forename: T
authors.initials: T
authors.lastname: Wilusz
mesh_terms: 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
chemical_list: D014361:Trypsin Inhibitors; D002918:Chymotrypsin; D010196:Pancreatic Elastase