Figure 3 | Scientific Reports

Figure 3

From: Increasing thermal stability and improving biodistribution of VEGFR2-binding affibody molecules by a combination of in silico and directed evolution approaches

Figure 3

Stability and affinity of monomers generated by PROSS. (a) Thermal stability of PROSS variants, determined by variable temperature CD spectroscopy with red representing the original binders. Shown as fraction unfolded. (b) Rate scale plots of variants from selection, affinity constants determined by Biacore 8 K measurement. Rate scale plots were created with www.affinity-avidity.com, provided by Dynamic Biosensors. (c) Thermal stability of PROSS single-mutant variants, determined by variable temperature CD spectroscopy with red representing the original binders. Shown as fraction unfolded (d) Schematic representation of affibody molecule with residue mutations generated by PROSS shown in blue and residues locked to preserve the target-binding interface shown in purple.

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