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Recombinant Spider Silk as Mediator for One-Step, Chemical-Free Surface Biofunctionalization
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.
Uppsala Univ, Ångström Lab, Solid State Elect, Uppsala Box 534, SE-75121 Uppsala, Sweden..
KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Protein Science, Protein Engineering.ORCID iD: 0000-0001-7596-5075
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2018 (English)In: Advanced Functional Materials, ISSN 1616-301X, E-ISSN 1616-3028, Vol. 28, no 21, article id 1800206Article in journal (Refereed) Published
Abstract [en]

A unique strategy for effective, versatile, and facile surface biofunctionalization employing a recombinant spider silk protein genetically functionalized with the antibody-binding Z domain (Z-4RepCT) is reported. It is demonstrated that Z-silk can be applied to a variety of materials and platform designs as a truly one-step and chemical-free surface modification that site specifically captures antibodies while simultaneously reducing nonspecific adsorption. As a model surface, SiO2 is used to optimize and characterize Z-silk performance compared to the Z domain immobilized by a standard silanization method. First, Z-silk adsorption is investigated and verified its biofunctionality in a long-term stability experiment. To assess the binding capacity and protein-protein interaction stability of Z-silk, the coating is used to capture human antibodies in various assay formats. An eightfold higher binding capacity and 40-fold lower detection limit are obtained in the immunofluorescence assay, and the complex stability of captured antibodies is shown to be improved by a factor of 20. Applicability of Z-silk to functionalize microfluidic devices is demonstrated by antibody detection in an electrokinetic microcapillary biosensor. To test Z-silk for biomarker applications, real-time detection and quantification of human immunoglobulin G are performed in a plasma sample and C1q capture from human serum using an anti-C1q antibody.

Place, publisher, year, edition, pages
WILEY-V C H VERLAG GMBH , 2018. Vol. 28, no 21, article id 1800206
Keywords [en]
biomarker, biosensing, C1q, surface biofunctionalization, Z-silk
National Category
Analytical Chemistry
Identifiers
URN: urn:nbn:se:kth:diva-231216DOI: 10.1002/adfm.201800206ISI: 000434030500011Scopus ID: 2-s2.0-85047860287OAI: oai:DiVA.org:kth-231216DiVA, id: diva2:1228573
Note

QC 20180628

Available from: 2018-06-28 Created: 2018-06-28 Last updated: 2018-11-23Bibliographically approved

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Jansson, RonnieNilebäck, LinneaBehnam, KiarashLinnros, JanHedhammar, MyEriksson Karlström, Amelie

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Horak, JosefJansson, RonnieNilebäck, LinneaBehnam, KiarashLinnros, JanHedhammar, MyEriksson Karlström, Amelie
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