Fig. 1

Haddock solvated docking shows binding of hNET-derived peptides to hNET in silico. Best-predicted binding pose of GASNGINAYL peptide with hNET-M model (a) and hNET-S model (b), and for SLWERLAYGI peptide with hNET-M model (c) and hNET-S model (d). Peptides are shown with minimal backbone for clarity (light blue—backbone, red—oxygen, dark blue—nitrogen). hNET ribbon and surface are shown in salmon-pink. hNET side-chains within 3 Å distance from peptides are labeled and shown in green. e Non-bonded energies showing major contribution of electrostatic interactions to the binding. f Structure–Structure alignment of top four binding poses indicating similar mode of interaction. The overlapping sequence between the homing peptides is attributed to six homologous residues (highlighted boxes) at the same binding site. Root-mean square-deviations (RMSD) are shown in figurative grey bars for backbone (Ca) and for both backbone and side-chains (Full). The alignment can serve as a roadmap for designing derived sequences of hNET homing peptides