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- W4241010387 abstract "Highly potent bifunctional inhibitors of Factor VIIa (FVIIa) were generated by linking two distinct peptides, recently shown to bind to two discrete exosites on the FVIIa protease domain [Dennis, Eigenbrot, Skelton, Ultsch, Santell, Dwyer, O'Connell and Lazarus (2000) Nature (London) 404, 465–470; Dennis, Roberge, Quan and Lazarus (2001) Biochemistry 40, 9513–9521; Roberge, Santell, Dennis, Eigenbrot, Dwyer and Lazarus (2001) Biochemistry 40, 9522–9531]. Fusion peptides consisting of an N-terminal A-series peptide followed by flexible linkers, an E-series peptide, and the Z-domain of protein A were expressed in Escherichia coli and purified using IgG—Sepharose affinity chromatography. The fusion peptides were potent anticoagulants and had steep concentration dependence curves in tissue factor-dependent prothrombin time (PT) assays in comparison to the individual peptides or their noncovalent combination. This phenomenon was dependent on the length of the linker joining the A- and E-peptides. The fusion of the peptides increased the extent of inhibition of Factor X (FX) activation to 100% at saturating peptide concentrations, but did not improve the binding affinity for Factor VIIa (FVIIa) at the A- and E- binding sites or the IC50 for the inhibition of FX activation. Differences between the peptides in the PT fold prolongation in normal and FVII-deficient plasma, in conjunction with the inhibition of 125I-FVII activation, suggest that the enhanced effects of the fusion peptides involve the inhibition of FVII autoactivation." @default.
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- W4241010387 date "2002-04-08" @default.
- W4241010387 modified "2023-09-30" @default.
- W4241010387 title "Fusion of two distinct peptide exosite inhibitors of Factor VIIa" @default.
- W4241010387 doi "https://doi.org/10.1042/bj3630387" @default.
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