Specific adsorption of histidine-tagged proteins on silica surfaces modified with Ni2+/NTA-derivatized poly(ethylene glycol)
DC Field | Value | Language |
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dc.contributor.author | Kang, Eunah | - |
dc.contributor.author | Park, Jin-Won | - |
dc.contributor.author | McClellan, Scott J. | - |
dc.contributor.author | Kim, Jong-Mok | - |
dc.contributor.author | Holland, David P. | - |
dc.contributor.author | Lee, Gil U. | - |
dc.contributor.author | Franses, Elias I. | - |
dc.contributor.author | Park, Kinam | - |
dc.contributor.author | Thompson, David H. | - |
dc.date.accessioned | 2021-07-30T07:40:21Z | - |
dc.date.available | 2021-07-30T07:40:21Z | - |
dc.date.issued | 2007-05 | - |
dc.identifier.issn | 0743-7463 | - |
dc.identifier.issn | 1520-5827 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/48022 | - |
dc.description.abstract | Silica surfaces modified with nitrilotriacetic acid (NTA)-polyethylene glycol (PEG) derivatives were used to immobilize hexahistidine-tagged green fluorescent protein (His(6)-GFP), biotin/streptavidin-AlexaFluor555 (His(6)-biotin/SA-AF), and gramicidin A-containing vesicles (His(6)-gA). Three types of surface-reactive PEG derivatives-NTA-PEG3400-Si(OMe)(3), NTA-PEG3400-vinylsulfone, and mPEG5000-Si(OMe)(3) (control)-were grafted onto silica and tested for their ability to capture His(6)-tag species via His(6)/Ni2+/NTA chelation. The composition and thicknesses of the PEG-modified surfaces were characterized using X-ray photoelectron spectroscopy, contact angle, and ellipsometry. Protein capture efficiencies of the NTA-PEG-grafted surfaces were evaluated by measuring fluorescence intensities of these surfaces after exposure to His(6)-tag species. XPS and ellipsometry data indicate that surface adsorption occurs via specific interactions between the His(6)-tag and the Ni2+/NTA-PEG-grafted surface. Protein immobilization was most effective for NTA-PEG3400-Si(OMe)(3)-modified surfaces, with maximal areal densities achieved at 45 pmol/cm(2) for His(6)-GFP and 95 fmol/cm(2) for His(6)-biotin/SA-AF. Lipid vesicles containing His(6)-gA in a 1:375 gA/lipid ratio could also be immobilized on Ni2+/NTA-PEG3400-Si(OMe)(3)-modified surfaces at 0.5 mM total lipid. Our results suggest that NTA-PEG-Si(OMe)(3) conjugates may be useful tools for immobilizing His(6)-tag proteins on solid surfaces to produce protein-functionalized surfaces. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Specific adsorption of histidine-tagged proteins on silica surfaces modified with Ni2+/NTA-derivatized poly(ethylene glycol) | - |
dc.type | Article | - |
dc.identifier.doi | 10.1021/la063719e | - |
dc.identifier.bibliographicCitation | LANGMUIR, v.23, no.11, pp 6281 - 6288 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000246456700062 | - |
dc.identifier.scopusid | 2-s2.0-34249875382 | - |
dc.citation.endPage | 6288 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 6281 | - |
dc.citation.title | LANGMUIR | - |
dc.citation.volume | 23 | - |
dc.type.docType | Article | - |
dc.publisher.location | 미국 | - |
dc.subject.keywordPlus | SELF-ASSEMBLED MONOLAYERS | - |
dc.subject.keywordPlus | NICOTINIC ACETYLCHOLINE-RECEPTOR | - |
dc.subject.keywordPlus | TETHERED LIPID-MEMBRANES | - |
dc.subject.keywordPlus | PLASMON RESONANCE | - |
dc.subject.keywordPlus | GOLD SURFACES | - |
dc.subject.keywordPlus | FUNCTIONAL IMMOBILIZATION | - |
dc.subject.keywordPlus | REVERSIBLE IMMOBILIZATION | - |
dc.subject.keywordPlus | SUPPORTED MEMBRANES | - |
dc.subject.keywordPlus | GRAFTING DENSITY | - |
dc.subject.keywordPlus | BILAYERS | - |
dc.relation.journalResearchArea | Chemistry | - |
dc.relation.journalResearchArea | Materials Science | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Multidisciplinary | - |
dc.relation.journalWebOfScienceCategory | Chemistry, Physical | - |
dc.relation.journalWebOfScienceCategory | Materials Science, Multidisciplinary | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
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