Fig. 7.

(A) ΔΔG_{bind(Rosetta)} (REU) of all designed peptides obtained from Rosetta. Note that the ΔΔG_bind was calculated using the following equation: ΔΔG_bind = ΔG_bind (mutant) – ΔG_bind (wild-type). (B) ΔG_bind (kcal/mol) of all designed peptides obtained from MM-PBSA method. (C) Representative structures of the two most promising peptides CendR_R683G and CendR_A684M showing the ligand orientation in NRP1 b1 domain drawn from the last MD snapshot. (D) $\mathrm{\Delta }{G}_{\text{bind}}^{\text{residue}}$ of CendR_WT, CendR_R683G, and CendR_A684M contributing to the binding of NRP1. (E) $\mathrm{\Delta }{G}_{\text{bind}}^{\text{residue}}$ of NRP1 contributing to the binding of CendR_WT, CendR_R683G, and CendR_A684M. (F) Percentage of H-bond occupation of NRP1 contributing to the binding of (left) CendR_WT, (middle) CendR_R683G, and (right) CendR_A684M. %H-bond occupation (%H-bond_oc) was classified into four levels: (i) strong H-bond (%H-bond_oc of > 75%), (ii) medium H-bond (75% ≥ %H-bond_oc > 50%), and (iii) weak H-bond (50% ≥ %H-bond_oc > 10%).