Surface-independent and oriented immobilization of antibody via one-step polydopamine/protein G coating: application to influenza virus immunoassay

Cited 22 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorJeong Moon-
dc.contributor.authorJihyun Byun-
dc.contributor.authorHongki Kim-
dc.contributor.authorJinyoung Jeong-
dc.contributor.authorEun-Kyung Lim-
dc.contributor.authorJuyeon Jung-
dc.contributor.authorS Cho-
dc.contributor.authorW K Cho-
dc.contributor.authorTaejoon Kang-
dc.date.accessioned2019-07-10T01:23:35Z-
dc.date.available2019-07-10T01:23:35Z-
dc.date.issued2019-
dc.identifier.issn1616-5187-
dc.identifier.uri10.1002/mabi.201800486ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/18816-
dc.description.abstractFor the construction of high-performance biosensor, it is important to interface bioreceptors with the sensor surface densely and in the optimal orientation. Herein, a simple surface modification method that can optimally immobilize antibodies onto various kinds of surfaces is reported. For the surface modification, a mixture of polydopamine (PDA) and protein G was employed. PDA is a representative mussel-inspired polymer, and protein G is an immunoglobulin-binding protein that enables an antibody to have an optimal orientation. The surface characteristics of PDA/Protein G mixture-coated substrates are analyzed and the PDA/protein G ratio is optimized to maximize the antibody binding efficiency. Moreover, the antibody-immobilized substrates are applied to the detection of influenza viruses with the naked eye, providing a detection limit of 2.9 × 103 pfu mL-1. Importantly, the several substrates (glass, SiO2, Si, Al2O3, polyethylene terephthalate, polyethylene, polypropylene, and paper) can be modified by simple incubation with the mixture of PDA/protein G, and then the anti-influenza A H1N1 antibodies can be immobilized on the substrates successfully. Regardless of the substrate, the influenza viruses are detectable after the sandwich immunoreaction and silver enhancement procedure. It is anticipated that the developed PDA/protein G coating method will extend the range of applicable materials for biosensing.-
dc.publisherWiley-
dc.titleSurface-independent and oriented immobilization of antibody via one-step polydopamine/protein G coating: application to influenza virus immunoassay-
dc.title.alternativeSurface-independent and oriented immobilization of antibody via one-step polydopamine/protein G coating: application to influenza virus immunoassay-
dc.typeArticle-
dc.citation.titleMacromolecular Bioscience-
dc.citation.number6-
dc.citation.endPage1800486-
dc.citation.startPage1800486-
dc.citation.volume19-
dc.contributor.affiliatedAuthorJeong Moon-
dc.contributor.affiliatedAuthorJihyun Byun-
dc.contributor.affiliatedAuthorHongki Kim-
dc.contributor.affiliatedAuthorJinyoung Jeong-
dc.contributor.affiliatedAuthorEun-Kyung Lim-
dc.contributor.affiliatedAuthorJuyeon Jung-
dc.contributor.affiliatedAuthorTaejoon Kang-
dc.contributor.alternativeName문정-
dc.contributor.alternativeName변지현-
dc.contributor.alternativeName김홍기-
dc.contributor.alternativeName정진영-
dc.contributor.alternativeName임은경-
dc.contributor.alternativeName정주연-
dc.contributor.alternativeName조수정-
dc.contributor.alternativeName조우경-
dc.contributor.alternativeName강태준-
dc.identifier.bibliographicCitationMacromolecular Bioscience, vol. 19, no. 6, pp. 1800486-1800486-
dc.identifier.doi10.1002/mabi.201800486-
dc.subject.keywordantibody immobilization-
dc.subject.keywordimmunoassay-
dc.subject.keywordpolydopamine-
dc.subject.keywordprotein G-
dc.subject.keywordsurface modification-
dc.subject.localAntibody Immobilization-
dc.subject.localAntibody immobilization-
dc.subject.localantibody immobilization-
dc.subject.localImmunoassay-
dc.subject.localImmunoassays-
dc.subject.localimmunoassay-
dc.subject.localpolydopamine-
dc.subject.localPolydopamine-
dc.subject.localProtein G-
dc.subject.localprotein G-
dc.subject.localSurface modification-
dc.subject.localsurface modification-
dc.subject.localSurface modifcation-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Environmental diseases research center > 1. Journal Articles
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.