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SFTI currently protects data transferred by all the major U.S. stock markets.
Although SFTI-FCQR Asn14 was less stable than SFTI-FCQR Asp14 in culture with prostate cancer cells, it was sufficiently resistant to degradation, highlighting the robustness of the SFTI scaffold.
To examine the impact of modifying the contact β-sheet of SFTI on the distribution of internal hydrogen bonds, corresponding simulations were performed on KLK4 (PDB ID 2BDG) in complex with a model of SFTI-FCQR Asp14.
To harness the favourable structural features of SFTI-1 and redirect inhibition towards KLK4, the contact β-sheet of SFTI was recently re-engineered using a sparse matrix peptide library to guide amino acid substitutions.
However, the constrained geometry of SFTI prevents the use of linear peptide libraries to optimise interactions beyond the P1 P4 residues, while producing a synthetic SFTI library is prohibitively costly and time consuming.
The prominent role of internal hydrogen bonding in maintaining canonical loop rigidity is not only limited to the SFTI scaffold.
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Trypsin inhibitor SFTI-1 is the smallest and the most potent among BBI inhibitors.
We further identified chemical and structural features of SFTI-1 and its analogues that underpin their inhibitory activity.
SFTI-1 is a recently discovered cyclic peptide trypsin inhibitor from sunflower seeds comprising 14 amino acid residues.
Cells were treated ±1 µM inhibitor (SFTI-FCQR Asn14 or SFTI-FCQR Lys14) in fresh serum-containing media.
SFTI-1 binds to target proteases by an extended β-sheet across the P1-P4 residues to form a tight binding complex (trypsin/SFTI-1 Ki = 0.1 nM) [21].
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