Grafting of material-binding function into antibodies. Functionalization by peptide grafting

Takamitsu Hattori, Mitsuo Umetsu, Takeshi Nakanishi, Kouhei Tsumoto, Satoshi Ohara, Hiroya Abe, Makio Naito, Ryutaro Asano, Tadafumi Adschiri, Izumi Kumagai

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)


Quite recently, a few antibodies against bulk material surface have been selected from a human repertoire antibody library, and they are attracting immense interest in the bottom-up integration of nanomaterials. Here, we constructed antibody fragments with binding affinity and specificity for nonbiological inorganic material surfaces by grafting material-binding peptides into loops of the complementarity determining region (CDR) of antibodies. Loops were replaced by peptides with affinity for zinc oxide and silver material surfaces. Selection of CDR loop for replacement was critical to the functionalization of the grafted fragments; the grafting of material-binding peptide into the CDR2 loop functionalized the antibody fragments with the same affinity and selectivity as the peptides used. Structural insight on the scaffold fragment used implies that material-binding peptide should be grafted onto the most exposed CDR loop on scaffold fragment. We show that the CDR-grafting technique leads to a build-up creation of the antibody with affinity for nonbiological materials.

Original languageEnglish
Pages (from-to)751-757
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 2008 Jan 25


  • Antibody
  • Material-binding protein
  • Peptide-grafting


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