Protein-ligand interactions at poly(amidoamine) dendrimer monolayers on gold

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dc.contributor.authorHong M.Y.ko
dc.contributor.authorYoon H.C.ko
dc.contributor.authorKim, Hak-Sungko
dc.date.accessioned2009-12-07T01:38:36Z-
dc.date.available2009-12-07T01:38:36Z-
dc.date.created2012-02-06-
dc.date.created2012-02-06-
dc.date.issued2003-01-
dc.identifier.citationLANGMUIR, v.19, no.2, pp.416 - 421-
dc.identifier.issn0743-7463-
dc.identifier.urihttp://hdl.handle.net/10203/14252-
dc.description.abstractAvidin-biotin interactions as a typical protein-ligand model were investigated on the monolayers of a fourth-generation poly(amidoamine) dendrimer that were constructed on the self-assembled monolayers (SAMs) of 11-mercaptoundecanoic acid (MUA) on gold. Surface plasmon resonance (SPR) spectroscopic analysis revealed a resonance angle shift of 0.34degrees +/- 0.03degrees for the formation of dendrimer monolayers on reactive SAMs, which indicates that about 89% of the gold surface is covered with dendrimer molecules. The dendrimer monolayers were functionalized with biotin, and the efficacy of dendrimer monolayers as a biomolecular interface was evaluated in terms of the surface density of biotin ligands and the avidin binding level. For comparisons, the mixed SAMs and polymeric layers of poly-I.-lysine (PLL) on MUA SAMs were prepared and examined by a similar procedure. The specific binding of avidin to the biotinylated dendrimer monolayers, approached a surface density of 5.0 +/- 0.2 ng(.)mm(-2), which corresponds to about 88% surface coverage by avidin, showing a much higher level than those from mixed SAMs (2.3 +/- 0.1 ng(.)mm(-2)) and PLL layers (3.2 +/- 0.2 ng(.)mm(-2)). Interestingly, the fully biotinylated dendrimer monolayers gave rise to efficient avidin-biotin interactions, resulting in about 80% of the maximum avidin binding level, even under the condition that a serious steric hindrance would occur due to densely packed biotin ligands. These results strongly imply that efficient avidin-biotin interaction originates from a structural feature of dendrimer monolayers such as a surface exposure of derivatized biotin ligands and a corrugated surface.-
dc.languageEnglish-
dc.language.isoen_USen
dc.publisherAMER CHEMICAL SOC-
dc.subjectSELF-ASSEMBLED MONOLAYERS-
dc.subjectSURFACE-DENSITY-
dc.subjectAMINE GROUP-
dc.subjectPHOTOELECTRON-SPECTROSCOPY-
dc.subjectPOLY(L-LYSINE) MONOLAYERS-
dc.subjectMOLECULAR RECOGNITION-
dc.subjectGENE-EXPRESSION-
dc.subjectMETAL-OXIDES-
dc.subjectTHIN-LAYERS-
dc.subjectMICROARRAYS-
dc.titleProtein-ligand interactions at poly(amidoamine) dendrimer monolayers on gold-
dc.typeArticle-
dc.identifier.wosid000180519200030-
dc.identifier.scopusid2-s2.0-0037457866-
dc.type.rimsART-
dc.citation.volume19-
dc.citation.issue2-
dc.citation.beginningpage416-
dc.citation.endingpage421-
dc.citation.publicationnameLANGMUIR-
dc.embargo.liftdate9999-12-31-
dc.embargo.terms9999-12-31-
dc.contributor.localauthorKim, Hak-Sung-
dc.contributor.nonIdAuthorHong M.Y.-
dc.contributor.nonIdAuthorYoon H.C.-
dc.type.journalArticleArticle-
dc.subject.keywordPlusSELF-ASSEMBLED MONOLAYERS-
dc.subject.keywordPlusSURFACE-DENSITY-
dc.subject.keywordPlusAMINE GROUP-
dc.subject.keywordPlusPHOTOELECTRON-SPECTROSCOPY-
dc.subject.keywordPlusPOLY(L-LYSINE) MONOLAYERS-
dc.subject.keywordPlusMOLECULAR RECOGNITION-
dc.subject.keywordPlusGENE-EXPRESSION-
dc.subject.keywordPlusMETAL-OXIDES-
dc.subject.keywordPlusTHIN-LAYERS-
dc.subject.keywordPlusMICROARRAYS-
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