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Nanoparticles with affinity for biopolymer: Bioassisted room-temperature selective multistacking of inorganic particles on biopolymer film
Umetsu, Mitsuo; Hattori, Takamitsu; Kikuchi, Shinsuke; Muto, Itsuki; Nakanishi, Takeshi; Watanabe, Hideki; Kumagai, Izumi
Recently, we selected the antibody fragment with high affinity for the biopolymer film of polyhydroxybutyrate (PHB) from human antibody fragment libraries. In this Study. we functionalized CdSe quantum clot (QD) nanoparticles by orderly conjugating the anti-PHB antibody fragments to perform spontaneous and selective stacking of inorganic particles on PHB-coated plates in neutral solutions at room temperature. Surface plasmon resonance analysis showed that the orderly clustering of anti-PHB antibody fragment on QD particles led to no dissociation of QD on PHB-coated plates. indicating the availability of avidity effect. The strong spontaneous immobilization using biomolecular recognition enabled stepwise stacking of inorganic particles oil PHB-coated plates only by mixing operation in neutral Solutions at room temperature. We show the potential of recombinant anti-material antibody fragments for the bottom-up stacking procedures for hybrid assembly.
ISI:000261432200014
ISSN: 0884-2914
CID: 2773582
Bio-assisted conformation control of inorganic materials by Peptide Engineering [Meeting Abstract]
Umetsu, Mitsuo; Togashi, Takanari; Yokoo, Nozomi; Hattori, Takamitsu; Ohara, Satoshi; Adschiri, Tadafumi
ISI:000259026900625
ISSN: 1075-2617
CID: 2773592
Grafting of material-binding function into antibodies Functionalization by peptide grafting
Hattori, Takamitsu; Umetsu, Mitsuo; Nakanishi, Takeshi; Tsumoto, Kouhei; Ohara, Satoshi; Abe, Hiroya; Naito, Makio; Asano, Ryutaro; Adschiri, Tadafumi; Kumagai, Izumi
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.
PMID: 18039464
ISSN: 1090-2104
CID: 2773562
Decline of anti-DP107 antibody associated with clinical progression [Letter]
Hattori, T; Komoda, H; Pahwa, S; Tateyama, M; Zhang, X; Xu, Y; Oguma, S; Tamamura, H; Fujii, N; Fukutake, K; Uchiyama, T
PMID: 9727582
ISSN: 0269-9370
CID: 3778152