Peptide Nanofibers Modified with a Protein by Using Designed Anchor Molecules Bearing Hydrophobic and Functional Moieties

Self‐assembly of peptides and proteins is a key feature of biological functions. Short amphiphilic peptides designed with a β‐sheet structure can form sophisticated nanofiber structures, and the fibers are available as nanomaterials for arranging biomolecules. Peptide FI (H‐PKFKIIEFEP‐OH) self‐assembles into nanofibers with a coiled fine structure, as reported in our previous work. We have constructed anchor molecules that have both a binding moiety for the fiber structure and a functional unit capable of capturing target molecules, with the purpose of arranging proteins on the designed peptide nanofibers. Designed anchors containing an alkyl chain as a binding unit and biotin as a functional moiety were found to bind to peptide fibers FI and F2i (H‐ALEAKFAAFEAKLA‐NH 2 ). The surface‐exposed biotin moiety on the fibers could capture an anti‐biotin antibody. Moreover, hydrophobic dipeptide anchor units composed of iminodiacetate connected to Phe–Phe or Ile–Ile and a peptide composed of six histidine residues connected to biotin could also connect FI peptide fibers to the anti‐biotin antibody through the chelation of Ni 2+ ions. This strategy of using designed anchors opens a novel approach to constructing nanoscale protein arrays on peptide nanomaterials.