Synthesis and evaluation of the sunflower derived trypsin inhibitor as a potent inhibitor of the type II transmembrane serine protease, matriptase.
We report here the synthesis of a 14-amino acid long bicyclic peptide, previously isolated from sunflower seeds. This peptide, termed sunflower trypsin inhibitor (SFTI-1), is one of the most potent naturally occurring small-molecule trypsin inhibitors. In addition to inhibiting trypsin, the synthetic SFTI-1 is also a very potent inhibitor, with a K(i) of 0.92nM, of the recently identified epithelial serine protease, termed 'matriptase'.
Long
Y Q
YQ
Laboratory of Medicinal Chemistry, National Cancer Institute, NIH, FCRDC, 376/208, PO Box B, Frederick, MD 21702, USA.
Lee
S L
SL
Lin
C Y
CY
Enyedy
I J
IJ
Wang
S
S
Li
P
P
Dickson
R B
RB
Roller
P P
PP
D000595:Amino Acid Sequence; D001671:Biochemistry / Q000379:methods; D006368:Helianthus / Q000737:chemistry; D008958:Models, Molecular; D010456:Peptides, Cyclic / Q000737:chemistry* / Q000494:pharmacology*; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry / Q000187:drug effects*; D015842:Serine Proteinase Inhibitors / Q000737:chemistry* / Q000494:pharmacology*; D014357:Trypsin / Q000737:chemistry / Q000187:drug effects* / Q000494:pharmacology
D010456:Peptides, Cyclic; C448501:SFTI-1 peptide, sunflower; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; C485595:matriptase; D014357:Trypsin