Beilstein J. Org. Chem.2015,11, 701–706, doi:10.3762/bjoc.11.80
which demonstrates that the new carrier provides a venue for the future inhibition of proline-rich sequence recognition by FBP21 during assembly of the spliceosome.
Keywords: FBP21-tWW; isothermal titration calorimetry; multivalent polymers; polyglycerol peptide conjugates; proline-rich sequence
endothelial growth factor (VEGF). In the same study, the natural compound borrelidin was suggested to confer its splicing inhibition function by directly binding to the WW domains of FBP21 [6]. Here, we have taken a different approach to inhibit binding of FBP21-tWW to proline-rich sequences in the
the interaction between hPG-peptide conjugate 2 and FBP21-tWW was measured by isothermal titration calorimetry (ITC) and compared to the KD of the interaction between the monovalent peptide and FBP21-tWW to analyze if multivalent display in form of the hPG-peptide conjugate 2 increases binding
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Graphical Abstract
Figure 1:
Phage display was used to find an optimized binding partner for FBP21-tWW. A) Schematic representat...