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1.
Langmuir ; 35(8): 3067-3076, 2019 02 26.
Artículo en Inglés | MEDLINE | ID: mdl-30689940

RESUMEN

Recent advances in biotechnology have enabled the generation of antibodies with high affinity for the surfaces of specific inorganic materials. Herein, we report the synthesis of functional materials from multiple nanomaterials by using a small bispecific antibody recombinantly constructed from gold-binding and ZnO-binding antibody fragments. The bispecific antibody-mediated spontaneous linkage of gold and ZnO nanoparticles forms a binary gold-ZnO nanoparticle composite membrane. The relatively low melting point of the gold nanoparticles and the solubility of ZnO in dilute acidic solution then allowed for the bottom-up synthesis of a nanoporous gold membrane by means of a low-energy, low-environmental-load protocol. The nanoporous gold membrane showed high catalytic activity for the reduction of p-nitrophenol to p-aminophenol by sodium borohydride. Here, we show the potential utility of nanoparticle pairing mediated by bispecific antibodies for the bottom-up construction of nanostructured materials from multiple nanomaterials.


Asunto(s)
Anticuerpos Biespecíficos/química , Diseño de Fármacos , Nanopartículas/química , Nanotecnología , Catálisis , Dimerización , Oro/química , Fragmentos de Inmunoglobulinas/química , Membranas Artificiales , Porosidad , Óxido de Zinc/química
2.
J Biol Chem ; 285(10): 7784-93, 2010 Mar 05.
Artículo en Inglés | MEDLINE | ID: mdl-20044483

RESUMEN

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.


Asunto(s)
Anticuerpos , Afinidad de Anticuerpos , Péptidos/inmunología , Ingeniería de Proteínas/métodos , Adsorción , Óxido de Aluminio/química , Óxido de Aluminio/inmunología , Secuencia de Aminoácidos , Animales , Anticuerpos/química , Anticuerpos/inmunología , Cobalto/química , Cobalto/inmunología , Humanos , Fragmentos de Inmunoglobulinas/química , Fragmentos de Inmunoglobulinas/genética , Fragmentos de Inmunoglobulinas/inmunología , Ratones , Modelos Moleculares , Datos de Secuencia Molecular , Nanotecnología , Óxidos/química , Óxidos/inmunología , Biblioteca de Péptidos , Péptidos/química , Péptidos/genética , Conformación Proteica , Propiedades de Superficie , Termodinámica , Óxido de Zinc/química , Óxido de Zinc/inmunología
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