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 inJournal of physical chemistry. C Vol. 119; no. 36; pp. 21035 - 21043
Main Authors Lin, Wayne, Insley, Thomas, Tuttle, Marcus D, Zhu, Lingyang, Berthold, Deborah A, Král, Petr, Rienstra, Chad M, Murphy, Catherine J
Format Journal Article
LanguageEnglish
Published United States American Chemical Society 10.09.2015
Subjects
protein adsorption
surface chemistry
protein orientation
Gold nanoparticles
α-synuclein
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Abstract 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.
AbstractList 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.
Gold nanoparticles (Au NPs) have attracted much attention due to their potential applications in nano-medicine. 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.
Author Tuttle, Marcus D
Lin, Wayne
Král, Petr
Rienstra, Chad M
Berthold, Deborah A
Murphy, Catherine J
Zhu, Lingyang
Insley, Thomas
AuthorAffiliation Department of Chemistry
University of Illinois at Chicago
Center for Biophysics and Computational Biology
School of Chemical Sciences
University of Illinois at Urbana−Champaign
Department of Biochemistry
Department of Physics
AuthorAffiliation_xml – name:
– name: Department of Chemistry
– name: School of Chemical Sciences
– name: Department of Physics
– name: Center for Biophysics and Computational Biology
– name: University of Illinois at Urbana−Champaign
– name: Department of Biochemistry
– name: University of Illinois at Chicago
– name: Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, Illinois, 60607, USA
– name: Department of Physics, University of Illinois at Chicago, 845 West Taylor Street, Chicago, Illinois, 60607, USA
– name: Center for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, 607 South Matthews Avenue, Urbana, Illinois, 61801, USA
– name: School of Chemical Sciences, University of Illinois at Urbana-Champaign, 505 South Matthews Avenue, Urbana, Illinois, 61801, USA
– name: Department of Chemistry, University of Illinois at Urbana-Champaign, 600 South Matthews Avenue, Urbana, Illinois, 61801, USA
– name: Department of Biochemistry, University of Illinois at Urbana-Champaign, 600 South Matthews Avenue, Urbana, Illinois, 61801, USA
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BackLink https://www.ncbi.nlm.nih.gov/pubmed/28626495$$D View this record in MEDLINE/PubMed
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Keywords protein adsorption
surface chemistry
protein orientation
Gold nanoparticles
α-synuclein
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Snippet Gold nanoparticles (Au NPs) have attracted much attention due to their potential applications in nanomedicine. While numerous studies have quantified...
Gold nanoparticles (Au NPs) have attracted much attention due to their potential applications in nano-medicine. While numerous studies have quantified...
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StartPage 21035
Title Control of Protein Orientation on Gold Nanoparticles
URI http://dx.doi.org/10.1021/acs.jpcc.5b07701
https://www.ncbi.nlm.nih.gov/pubmed/28626495
https://www.proquest.com/docview/1911202980/abstract/
https://pubmed.ncbi.nlm.nih.gov/PMC5472360
Volume 119
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