Control of Protein Orientation on Gold Nanoparticles
Gold nanoparticles (Au NPs) have attracted much attention due to their potential applications in nanomedicine. While numerous studies have quantified biomolecular adsorption to Au NPs in terms of equilibrium binding constants, far less is known about biomolecular orientation on nanoparticle surfaces...
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Published in | Journal of physical chemistry. C Vol. 119; no. 36; pp. 21035 - 21043 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
10.09.2015
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Subjects | |
Online Access | Get full text |
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Summary: | Gold nanoparticles (Au NPs) have attracted much attention due to their potential applications in nanomedicine. While numerous studies have quantified biomolecular adsorption to Au NPs in terms of equilibrium binding constants, far less is known about biomolecular orientation on nanoparticle surfaces. In this study, the binding of the protein α-synuclein to citrate and (16-mercaptohexadecyl)trimethylammonium bromide (MTAB)-coated 12 nm Au NPs is examined by heteronuclear single quantum coherence NMR spectroscopy to provide site-specific measurements of protein–nanoparticle binding. Molecular dynamics simulations support the orientation assignments, which show N-terminus binding to the Au NP for citrate-capped NPs and C-terminus binding for the MTAB-capped NPs. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1932-7447 1932-7455 |
DOI: | 10.1021/acs.jpcc.5b07701 |