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Sunflower trypsin inhibitor-1, proteolytic studies on a trypsin inhibitor peptide and its analogs.
Peptide Science, 2010AbstractSunflower trypsin inhibitor‐1 (SFTI‐1) is a 14 amino acid cyclic peptide from sunflower seeds, which possesses exceptionally potent trypsin‐inhibitory activity, and has promise as a stable peptide‐based drug template. Within its compact structure, SFTI‐1 combines a head‐to‐tail cyclized backbone and a disulfide bond.
M. Colgrave +4 more
semanticscholar +5 more sources
Journal of Food Measurement and Characterization, 2019
, Rani Anita, Anita Rani
exaly +2 more sources
, Rani Anita, Anita Rani
exaly +2 more sources
Journal of Gastroenterology, 2006
Trypsin activity is properly suppressed in the pancreatic acinar cells under normal conditions. A small amount of trypsinogen is converted to active trypsin and inactivated by pancreatic secretory trypsin inhibitor (PSTI), thereby preventing damage to pancreatic acinar cells as a first line of defense.
M. Hirota, M. Ohmuraya, H. Baba
semanticscholar +3 more sources
Trypsin activity is properly suppressed in the pancreatic acinar cells under normal conditions. A small amount of trypsinogen is converted to active trypsin and inactivated by pancreatic secretory trypsin inhibitor (PSTI), thereby preventing damage to pancreatic acinar cells as a first line of defense.
M. Hirota, M. Ohmuraya, H. Baba
semanticscholar +3 more sources
Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis
Journal of Photochemistry and Photobiology B: Biology, 2014L Bekale, P Chanphai, H A Tajmir-Riahi
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, 2020
Soymilk is becoming popular worldwide due to its nutritional benefits and the increasing demand for plant-based alternatives for cow's milk resulting from lactose intolerance and dairy allergy.
S. Vanga, Jin Wang, V. Raghavan
semanticscholar +1 more source
Soymilk is becoming popular worldwide due to its nutritional benefits and the increasing demand for plant-based alternatives for cow's milk resulting from lactose intolerance and dairy allergy.
S. Vanga, Jin Wang, V. Raghavan
semanticscholar +1 more source
Archives of Biochemistry and Biophysics, 1974
Abstract Fetuin per se is a moderately strong trypsin inhibitor of the temporary type and retains its antitryptic activity upon desialicization. It forms a reversible 1:1 complex with β-trypsin and is functionally homogeneous in this respect. Complex formation is an entropy-driven reaction evidently due to release of structured water associated ...
F, Galembeck, J R, Cann
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Abstract Fetuin per se is a moderately strong trypsin inhibitor of the temporary type and retains its antitryptic activity upon desialicization. It forms a reversible 1:1 complex with β-trypsin and is functionally homogeneous in this respect. Complex formation is an entropy-driven reaction evidently due to release of structured water associated ...
F, Galembeck, J R, Cann
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Current Protein & Peptide Science, 2004
SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K(i) value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors.
Korsinczky, M. L. J. +2 more
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SFTI-1 is a bicyclic 14 amino acid peptide that was originally isolated from the seeds of the sunflower Helianthus annuus. It is a potent inhibitor of trypsin, with a sub-nanomolar K(i) value and is homologous to the active site region of the well-known family of serine protease inhibitors known as the Bowman-Birk trypsin inhibitors.
Korsinczky, M. L. J. +2 more
openaire +5 more sources
Trypsin Uptake and Trypsin-Inhibitor Complexes
Biology of the Neonate, 2009Previous studies have suggested that both newborn animals and humans absorb intact proteases from the intestine in greater amounts than do adults. Absorbed proteases are rapidly complexed in plasma by several inhibitors which inactivate free proteases. In order to confirm increased intestinal uptake in newborns, we evaluated the plasma trypsin activity
Jeremiah J. Levine +3 more
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Trypsin inhibitors for the treatment of pancreatitis
Bioorganic & Medicinal Chemistry Letters, 2016Proline-based trypsin inhibitors occupying the S1-S2-S1' region were identified by an HTS screening campaign. It was discovered that truncation of the P1' moiety and appropriate extension into the S4 region led to highly potent trypsin inhibitors with excellent selectivity against related serine proteases and a favorable hERG profile.
Trixi, Brandl +8 more
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