Analogues of Cucurbita maxima trypsin inhibitor III (CMTI-III) with elastase inhibitory activity.
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.
Rózycki
J
J
Faculty of Chemistry, University of Gdańsk, Poland.
Kupryszewski
G
G
Rolka
K
K
Ragnarsson
U
U
Zbyryt
T
T
Krokoszyńska
I
I
Wilusz
T
T
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
C081870:CMTI protein, Cucurbita maxima; D010940:Plant Proteins; D015842:Serine Proteinase Inhibitors; D010196:Pancreatic Elastase