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

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

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  • Grafting of material-binding function into antibodies Functionalization by peptide grafting. Abstract Text:

    takamitsu hattoriTakamitsu Hattori,mitsuo umetsuMitsuo Umetsu,takeshi nakanishiTakeshi Nakanishi,kouhei tsumotoKouhei Tsumoto,satoshi oharaSatoshi Ohara,hiroya abeHiroya Abe,makio naitoMakio Naito,ryutaro asanoRyutaro Asano,tadafumi adschiriTadafumi Adschiri,izumi kumagaiIzumi Kumagai,takamitsu hattoriTakamitsu Hattori,mitsuo umetsuMitsuo Umetsu,takeshi nakanishiTakeshi Nakanishi,kouhei tsumotoKouhei Tsumoto,satoshi oharaSatoshi Ohara,hiroya abeHiroya Abe,makio naitoMakio Naito,ryutaro asanoRyutaro Asano,tadafumi adschiriTadafumi Adschiri,izumi kumagaiIzumi Kumagai,

    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.

    Grafting of material-binding function into antibodies Functionalization by peptide grafting. Publishing Authors By Initials

    t hattoriT Hattori,m umetsuM Umetsu,t nakanishiT Nakanishi,k tsumotoK Tsumoto,s oharaS Ohara,h abeH Abe,m naitoM Naito,r asanoR Asano,t adschiriT Adschiri,i kumagaiI Kumagai,t hattoriT Hattori,m umetsuM Umetsu,t nakanishiT Nakanishi,k tsumotoK Tsumoto,s oharaS Ohara,h abeH Abe,m naitoM Naito,r asanoR Asano,t adschiriT Adschiri,i kumagaiI Kumagai,

    For similar abstracts research abstracts see: abstracts research

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

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Biochemical and biophysical research communication

    VOLUME: 365

    Page Numbers: 751-7

    Journal Abbreviation: Biochem. Biophys. Res. Commun.

    ISSN: 1090-2104

    DAY: 26

    MONTH: 11

    YEAR: 2007

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

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    LANGUAGE: eng

    NlmUniqueID: 372516

    Grafting of material-binding function into antibodies Functionalization by peptide grafting. Keywords Mesh Terms:

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    Grant and Affiliation Information for Grafting of material-binding function into antibodies Functionalization by peptide grafting.

    AFFILIATION: Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Aoba 6-6-11-606, Aramaki, Aoba-ku, Sendai 980-8579, Japan.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Biochem Biophys Res Commun

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