title: Analogues of Cucurbita maxima trypsin inhibitor III (CMTI-III) with elastase inhibitory activity.
abstract: Three new CMTI-III analogues containing the Val residue in the reactive site (position 5) were synthesized by the solid-phase method. The analogues displayed an elastase inhibitory activity. It is shown that the removal of the N-terminal Arg residue and the introduction of the Gly-Pro-Gln tripeptide in the region 23-25 decreases the antielastase activity by two orders of magnitude. The removal of the disulfide bridge in positions 16-28 and the substitution of Ala for Cys16 and Gly for Cys28 decreases the activity (measured as Ka with HLE) by five orders of magnitude as compared with [Val5]CMTI-III.
authors.affiliation: Faculty of Chemistry, University of Gdańsk, Poland.
authors.forename: J
authors.initials: J
authors.lastname: Rózycki
authors.forename: G
authors.initials: G
authors.lastname: Kupryszewski
authors.forename: K
authors.initials: K
authors.lastname: Rolka
authors.forename: U
authors.initials: U
authors.lastname: Ragnarsson
authors.forename: T
authors.initials: T
authors.lastname: Zbyryt
authors.forename: I
authors.initials: I
authors.lastname: Krokoszyńska
authors.forename: T
authors.initials: T
authors.lastname: Wilusz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D006801:Humans; D008969:Molecular Sequence Data; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors*; D010940:Plant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D010946:Plants, Medicinal / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D013552:Swine
chemical_list: C081870:CMTI protein, Cucurbita maxima; D010940:Plant Proteins; D015842:Serine Proteinase Inhibitors; D010196:Pancreatic Elastase