Grafting of material-binding function into antibodies Functionalization by peptide grafting.
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.
Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-11-606, Aramaki, Aoba-ku, Sendai 980-8579, Japan.
Takamitsu
T
Hattori
Mitsuo
M
Umetsu
Takeshi
T
Nakanishi
Kouhei
K
Tsumoto
Satoshi
S
Ohara
Hiroya
H
Abe
Makio
M
Naito
Ryutaro
R
Asano
Tadafumi
T
Adschiri
Izumi
I
Kumagai
D000911:Antibodies, Monoclonal / Q000737:chemistry* / Q000276:immunology*; D001665:Binding Sites; D010455:Peptides / Q000737:chemistry* / Q000276:immunology*; D011485:Protein Binding; D015202:Protein Engineering / Q000379:methods*; D015034:Zinc Oxide / Q000737:chemistry* / Q000276:immunology*
D000911:Antibodies, Monoclonal; D010455:Peptides; D015034:Zinc Oxide