A fine-tuned composition of protein nanofibrils yields an upgraded functionality of displayed antibody binding domains.
Biotechnol J
; 12(6)2017 Jun.
Article
en En
| MEDLINE
| ID: mdl-28371185
Elevated performance of instruments and electronic devices is frequently attained through miniaturization of the involved components, which increases the number of functional units in a given volume. Analogously, to conquer the limitations of materials used for the purification of monoclonal antibodies and for the sensitivity of immunoassays, the support for capturing antibodies requires miniaturization. A suitable scaffold for this purpose are cross-ß structured protein nanofibrils, as they offer a superior surface area over volume ratio and because manipulation can be implemented genetically. To display the antibody binding Z-domain dimers (ZZ) along the surface of the fibrils and grant maximal accessibility to the functional units, the N-terminal fragments of the fibrillating translation release factor Sup35 or ureidosuccinate transporter Ure2, both from Saccharomyces cerevisae, are simultaneously fibrillated with the chimeric-proteins Sup35-ZZ and ZZ-Ure2, respectively. Optimization of the fibril composition yields a binding capacity of 1.8 mg antibody per mg fibril, which is a binding capacity that is almost 20-fold higher, compared to the commercially available affinity medium gold standard, protein A sepharose. This study lifts the craft of nanofibril functionalization to the next level, and offers a universal framework to improve biomaterials that rely on the display of functional proteins or enzymes.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Saccharomyces cerevisiae
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Priones
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Factores de Terminación de Péptidos
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Proteínas de Saccharomyces cerevisiae
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Glutatión Peroxidasa
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Anticuerpos Monoclonales
Idioma:
En
Revista:
Biotechnol J
Asunto de la revista:
BIOTECNOLOGIA
Año:
2017
Tipo del documento:
Article
País de afiliación:
Suecia
Pais de publicación:
Alemania