Human Anti-gold Antibodies
BIOFUNCTIONALIZATION OF GOLD NANOPARTICLES AND SURFACES WITH ANTI-GOLD ANTIBODIES*
- Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai 980-8579, Japan
- ↵1 To whom correspondence should be addressed: Aoba 6-6-11-606, Aoba-ku, Sendai 980-8579, Japan. Fax: 81-22-795-6164; E-mail: kmiz{at}kuma.che.tohoku.ac.jp.
Abstract
The interface molecules designed to exhibit molecular recognitions between different species have become attractive tools for the bottom-up fabrication and hybridization of nanostructured units. Here, we focus on antibodies with high binding ability and specificity to construct a novel biomolecule interface for recognizing an inorganic material. Careful selection from a phage-displayed library of variable region heavy and light Fv chains of human antibodies using enzyme-linked immunosorbent assay and surface plasmon resonance assay resulted in the identification of an antibody fragment, A14P-b2, with high affinity (KD = 1.7 nm) and specificity for gold materials. Our results indicated the potential usefulness of human antibody libraries and the effectiveness of the antibody framework for recognizing bulk material surfaces. Construction of bivalent and bispecific antibodies on the A14P-b2 platform with high affinity by means of fusion technology enabled the functionalization of gold nanoparticles and allowed selective protein accumulation on gold spots patterned on a silicon substrate. This type of antibody engineering is potentially applicable to bio-inspired materials and nanobiosensing.
Footnotes
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↵* This work was supported in part by a Grant-in-aid for Scientific Research and Grant-in-aid for Young Scientists from Japan Society for the Promotion of Science. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked “advertisement” in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
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The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1-S3.
- Received July 21, 2008.
- Revision received October 2, 2008.
- The American Society for Biochemistry and Molecular Biology, Inc.
