title: High affinity anti-inorganic material antibody generation by integrating graft and evolution technologies: potential of antibodies as biointerface molecules.
abstract: Recent advances in molecular evolution technology enabled us to identify peptides and antibodies with affinity for inorganic materials. In the field of nanotechnology, the use of the functional peptides and antibodies should aid the construction of interface molecules designed to spontaneously link different nanomaterials; however, few material-binding antibodies, which have much higher affinity than short peptides, have been identified. Here, we generated high affinity antibodies from material-binding peptides by integrating peptide-grafting and phage-display techniques. A material-binding peptide sequence was first grafted into an appropriate loop of the complementarity determining region (CDR) of a camel-type single variable antibody fragment to create a low affinity material-binding antibody. Application of a combinatorial library approach to another CDR loop in the low affinity antibody then clearly and steadily promoted affinity for a specific material surface. Thermodynamic analysis demonstrated that the enthalpy synergistic effect from grafted and selected CDR loops drastically increased the affinity for material surface, indicating the potential of antibody scaffold for creating high affinity small interface units. We show the availability of the construction of antibodies by integrating graft and evolution technology for various inorganic materials and the potential of high affinity material-binding antibodies in biointerface applications.
authors.affiliation: Department of Biomolecular Engineering, Graduate School of Engineering, Tohoku University, Sendai 980-8579, Japan.
authors.forename: Takamitsu
authors.initials: T
authors.lastname: Hattori
authors.forename: Mitsuo
authors.initials: M
authors.lastname: Umetsu
authors.forename: Takeshi
authors.initials: T
authors.lastname: Nakanishi
authors.forename: Takanari
authors.initials: T
authors.lastname: Togashi
authors.forename: Nozomi
authors.initials: N
authors.lastname: Yokoo
authors.forename: Hiroya
authors.initials: H
authors.lastname: Abe
authors.forename: Satoshi
authors.initials: S
authors.lastname: Ohara
authors.forename: Tadafumi
authors.initials: T
authors.lastname: Adschiri
authors.forename: Izumi
authors.initials: I
authors.lastname: Kumagai
mesh_terms: D000327:Adsorption; D000537:Aluminum Oxide / Q000737:chemistry / Q000276:immunology; D000595:Amino Acid Sequence; D000818:Animals; D000906:Antibodies / Q000737:chemistry / Q000276:immunology; D000915:Antibody Affinity; D003035:Cobalt / Q000737:chemistry / Q000276:immunology; D006801:Humans; D007128:Immunoglobulin Fragments / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D036103:Nanotechnology; D010087:Oxides / Q000737:chemistry / Q000276:immunology; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000276:immunology*; D011487:Protein Conformation; D015202:Protein Engineering / Q000379:methods*; D013499:Surface Properties; D013816:Thermodynamics; D015034:Zinc Oxide / Q000737:chemistry / Q000276:immunology
chemical_list: D000906:Antibodies; D007128:Immunoglobulin Fragments; D010087:Oxides; D019151:Peptide Library; D010455:Peptides; D003035:Cobalt; D000537:Aluminum Oxide; D015034:Zinc Oxide; C060728:cobalt oxide