Antibody-Binding, Antifouling Surface Coatings Based on Recombinant Expression of Zwitterionic EK Peptides

Development of antifouling films which selectively capture or target proteins of interest is essential for controlling interactions at the "bio/nano" interface. However, in order to synthesize biofunctional films from synthetic polymers that incorporate chemical "motifs" for surf...

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Détails bibliographiques
Publié dans:Langmuir : the ACS journal of surfaces and colloids. - 1985. - 35(2019), 5 vom: 05. Feb., Seite 1266-1272
Auteur principal: Walker, Julia A (Auteur)
Autres auteurs: Robinson, Kye J, Munro, Christopher, Gengenbach, Thomas, Muller, David A, Young, Paul R, Lua, Linda H L, Corrie, Simon R
Format: Article en ligne
Langue:English
Publié: 2019
Accès à la collection:Langmuir : the ACS journal of surfaces and colloids
Sujets:Journal Article Research Support, Non-U.S. Gov't Immobilized Proteins Immunoglobulin G Peptides Recombinant Proteins Viral Nonstructural Proteins Silicon Dioxide 7631-86-9
Description
Résumé:Development of antifouling films which selectively capture or target proteins of interest is essential for controlling interactions at the "bio/nano" interface. However, in order to synthesize biofunctional films from synthetic polymers that incorporate chemical "motifs" for surface immobilization, antifouling, and oriented biomolecule attachment, multiple reaction steps need to be carried out at the solid/liquid interface. EKx is a zwitterionic peptide that has previously been shown to have excellent antifouling properties. In this study, we recombinantly expressed EKx peptides and genetically encoded both surface attachment and antibody-binding motifs, before characterizing the resultant biopolymers by traditional methods. These peptides were then immobilized to organosilica nanoparticles for binding IgG, and subsequently capturing dengue NS1 as a model antigen from serum-containing solution. We found that a mixed layer of a short peptide (4.9 kDa) "backfilled" with a longer peptide terminated with an IgG-binding Z-domain (18 kDa) demonstrated selective capture of dengue NS1 protein down to ∼10 ng mL-1 in either PBS or 20% serum
Description:Date Completed 15.01.2020
Date Revised 15.01.2020
published: Print-Electronic
Citation Status MEDLINE
ISSN:1520-5827
DOI:10.1021/acs.langmuir.8b00810