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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1021/la400266u
|2 doi
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|a pubmed24n0752.xml
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|a (DE-627)NLM225676788
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|a (NLM)23477540
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Yang, Jie An
|e verfasserin
|4 aut
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| 245 |
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|a Study of wild-type α-synuclein binding and orientation on gold nanoparticles
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|c 2013
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 20.09.2013
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|a Date Revised 09.04.2022
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a The disruption of α-synuclein (α-syn) homeostasis in neurons is a potential cause of Parkinson's disease, which is manifested pathologically by the appearance of α-syn aggregates, or Lewy bodies. Treatments for neurological diseases are extremely limited. To study the potential use of gold nanoparticles (Au NPs) to limit α-syn misfolding, the binding and orientation of α-syn on Au NPs were investigated. α-Syn was determined to interact with 20 and 90 nm Au NPs via multilayered adsorption: a strong electrostatic interaction between α-syn and Au NPs in the hard corona and a weaker noncovalent protein-protein interaction in the soft corona. Spectroscopic and light-scattering titrations led to the determinations of binding constants for the Au NP α-syn coronas: for the hard corona on 20 nm Au NPs, the equilibrium association constant was 2.9 ± 1.1 × 10(9) M(-1) (for 360 ± 70 α-syn/NP), and on 90 nm Au NPs, the hard corona association constant was 9.5 ± 0.8 × 10(10) M(-1) (for 5300 ± 700 α-syn/NP). The binding of the soft corona was thermodynamically unfavorable and kinetically driven and was in constant exchange with "free" α-syn in solution. A protease digestion method was used to deduce the α-syn orientation and structure on Au NPs, revealing that α-syn absorbs onto negatively charged Au NPs via its N-terminus while apparently retaining its natively unstructured conformation. These results suggest that Au NPs could be used to sequester and regulate α-syn homeostasis
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|a Journal Article
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|a Research Support, U.S. Gov't, Non-P.H.S.
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|a alpha-Synuclein
|2 NLM
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| 650 |
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|a Gold
|2 NLM
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| 650 |
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|a 7440-57-5
|2 NLM
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|a Trypsin
|2 NLM
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|a EC 3.4.21.4
|2 NLM
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| 700 |
1 |
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|a Johnson, Brittany J
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Wu, Sway
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Woods, Wendy S
|e verfasserin
|4 aut
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| 700 |
1 |
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|a George, Julia M
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Murphy, Catherine J
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 29(2013), 14 vom: 09. Apr., Seite 4603-15
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:29
|g year:2013
|g number:14
|g day:09
|g month:04
|g pages:4603-15
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|u http://dx.doi.org/10.1021/la400266u
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