Peptide Nanofibers Modified with a Protein by Using Designed Anchor Molecules Bearing Hydrophobic and Functional Moieties |
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Authors: | Ayaka Miyachi Tsuyoshi Takahashi Dr Sachiko Matsumura Dr Hisakazu Mihara Prof |
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Institution: | Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Yokohama 226‐8501 (Japan), Fax: (+81)?45‐924‐5833 |
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Abstract: | 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‐NH2). 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 Ni2+ ions. This strategy of using designed anchors opens a novel approach to constructing nanoscale protein arrays on peptide nanomaterials. |
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Keywords: | electron microscopy nanostructures peptides proteins self‐assembly |
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