Antibody-binding, antifouling surface coatings based on recombinant expression of zwitterionic EK peptides

Julia A. Walker, Kye J. Robinson, Christopher Munro, Thomas Gengenbach, David A. Muller, Paul R. Young, Linda H.L. Lua, Simon R. Corrie

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)1266-1272
Number of pages7
JournalLangmuir
Volume35
Issue number5
DOIs
Publication statusPublished - 5 Feb 2019

Cite this

Walker, Julia A. ; Robinson, Kye J. ; Munro, Christopher ; Gengenbach, Thomas ; Muller, David A. ; Young, Paul R. ; Lua, Linda H.L. ; Corrie, Simon R. / Antibody-binding, antifouling surface coatings based on recombinant expression of zwitterionic EK peptides. In: Langmuir. 2019 ; Vol. 35, No. 5. pp. 1266-1272.
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abstract = "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.",
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Walker, JA, Robinson, KJ, Munro, C, Gengenbach, T, Muller, DA, Young, PR, Lua, LHL & Corrie, SR 2019, 'Antibody-binding, antifouling surface coatings based on recombinant expression of zwitterionic EK peptides', Langmuir, vol. 35, no. 5, pp. 1266-1272. https://doi.org/10.1021/acs.langmuir.8b00810

Antibody-binding, antifouling surface coatings based on recombinant expression of zwitterionic EK peptides. / Walker, Julia A.; Robinson, Kye J.; Munro, Christopher; Gengenbach, Thomas; Muller, David A.; Young, Paul R.; Lua, Linda H.L.; Corrie, Simon R.

In: Langmuir, Vol. 35, No. 5, 05.02.2019, p. 1266-1272.

Research output: Contribution to journalArticleResearchpeer-review

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AU - Corrie, Simon R.

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Walker JA, Robinson KJ, Munro C, Gengenbach T, Muller DA, Young PR et al. Antibody-binding, antifouling surface coatings based on recombinant expression of zwitterionic EK peptides. Langmuir. 2019 Feb 5;35(5):1266-1272. https://doi.org/10.1021/acs.langmuir.8b00810