Beilstein J. Org. Chem.2015,11, 837–847, doi:10.3762/bjoc.11.93
tandem WW-domain of formin-binding protein (FBP21). Polymer carriers were conjugated with 3–9 copies of the proline-rich decapeptide GPPPRGPPPR-NH2 (P1). Binding of the obtained peptide–polymerconjugates to the tandem WW-domain was investigated employing isothermal titration calorimetry (ITC) to
determine the binding affinity, the enthalpic and entropic contributions to free binding energy, and the stoichiometry of binding for all peptide–polymerconjugates. Binding affinities of all multivalent ligands were in the µM range, strongly amplified compared to the monovalent ligand P1 with a KD > 1 mM
precipitation. Experimental results were compared with parameters obtained from molecular dynamics simulations in order to understand the observed differences between the three carrier materials. In summary, the more rigid and condensed peptide–polymerconjugates based on the dextran scaffold seem to be
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Graphical Abstract
Figure 1:
Comparing the entropy loss during ligand–receptor interactions in dependence of the rigidity of the...