Abstract
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'.
Publication types
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Evaluation Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Biochemistry / methods
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Helianthus / chemistry
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Models, Molecular
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Peptides, Cyclic / chemistry*
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Peptides, Cyclic / pharmacology*
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Protein Conformation
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Serine Endopeptidases / chemistry
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Serine Endopeptidases / drug effects*
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Serine Proteinase Inhibitors / chemistry*
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Serine Proteinase Inhibitors / pharmacology*
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Trypsin / chemistry
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Trypsin / drug effects*
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Trypsin / pharmacology
Substances
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Peptides, Cyclic
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SFTI-1 peptide, sunflower
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Serine Proteinase Inhibitors
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Serine Endopeptidases
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matriptase
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Trypsin