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 language | English |
|---|---|
| Pages (from-to) | 1266-1272 |
| Number of pages | 7 |
| Journal | Langmuir |
| Volume | 35 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 5 Feb 2019 |
Cite this
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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 journal › Article › Research › peer-review
TY - JOUR
T1 - Antibody-binding, antifouling surface coatings based on recombinant expression of zwitterionic EK peptides
AU - Walker, Julia A.
AU - Robinson, Kye J.
AU - Munro, Christopher
AU - Gengenbach, Thomas
AU - Muller, David A.
AU - Young, Paul R.
AU - Lua, Linda H.L.
AU - Corrie, Simon R.
PY - 2019/2/5
Y1 - 2019/2/5
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85047750624&partnerID=8YFLogxK
U2 - 10.1021/acs.langmuir.8b00810
DO - 10.1021/acs.langmuir.8b00810
M3 - Article
VL - 35
SP - 1266
EP - 1272
JO - Langmuir: the ACS journal of surfaces and colloids
JF - Langmuir: the ACS journal of surfaces and colloids
SN - 0743-7463
IS - 5
ER -