DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hong M.Y. | ko |
dc.contributor.author | Yoon H.C. | ko |
dc.contributor.author | Kim, Hak-Sung | ko |
dc.date.accessioned | 2009-12-07T01:38:36Z | - |
dc.date.available | 2009-12-07T01:38:36Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-01 | - |
dc.identifier.citation | LANGMUIR, v.19, no.2, pp.416 - 421 | - |
dc.identifier.issn | 0743-7463 | - |
dc.identifier.uri | http://hdl.handle.net/10203/14252 | - |
dc.description.abstract | Avidin-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.language | English | - |
dc.language.iso | en_US | en |
dc.publisher | AMER CHEMICAL SOC | - |
dc.subject | SELF-ASSEMBLED MONOLAYERS | - |
dc.subject | SURFACE-DENSITY | - |
dc.subject | AMINE GROUP | - |
dc.subject | PHOTOELECTRON-SPECTROSCOPY | - |
dc.subject | POLY(L-LYSINE) MONOLAYERS | - |
dc.subject | MOLECULAR RECOGNITION | - |
dc.subject | GENE-EXPRESSION | - |
dc.subject | METAL-OXIDES | - |
dc.subject | THIN-LAYERS | - |
dc.subject | MICROARRAYS | - |
dc.title | Protein-ligand interactions at poly(amidoamine) dendrimer monolayers on gold | - |
dc.type | Article | - |
dc.identifier.wosid | 000180519200030 | - |
dc.identifier.scopusid | 2-s2.0-0037457866 | - |
dc.type.rims | ART | - |
dc.citation.volume | 19 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 416 | - |
dc.citation.endingpage | 421 | - |
dc.citation.publicationname | LANGMUIR | - |
dc.embargo.liftdate | 9999-12-31 | - |
dc.embargo.terms | 9999-12-31 | - |
dc.contributor.localauthor | Kim, Hak-Sung | - |
dc.contributor.nonIdAuthor | Hong M.Y. | - |
dc.contributor.nonIdAuthor | Yoon H.C. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | SELF-ASSEMBLED MONOLAYERS | - |
dc.subject.keywordPlus | SURFACE-DENSITY | - |
dc.subject.keywordPlus | AMINE GROUP | - |
dc.subject.keywordPlus | PHOTOELECTRON-SPECTROSCOPY | - |
dc.subject.keywordPlus | POLY(L-LYSINE) MONOLAYERS | - |
dc.subject.keywordPlus | MOLECULAR RECOGNITION | - |
dc.subject.keywordPlus | GENE-EXPRESSION | - |
dc.subject.keywordPlus | METAL-OXIDES | - |
dc.subject.keywordPlus | THIN-LAYERS | - |
dc.subject.keywordPlus | MICROARRAYS | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.