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231224s2012 xx |||||o 00| ||eng c |
| 024 |
7 |
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|a 10.1021/la203078w
|2 doi
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|a pubmed24n0713.xml
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|a (DE-627)NLM213847051
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|a (NLM)22168533
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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| 100 |
1 |
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|a Cabaleiro-Lago, C
|e verfasserin
|4 aut
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| 245 |
1 |
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|a The effect of nanoparticles on amyloid aggregation depends on the protein stability and intrinsic aggregation rate
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|c 2012
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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 09.07.2012
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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 Nanoparticles interfere with protein amyloid formation. Catalysis of the process may occur due to increased local protein concentration and nucleation on the nanoparticle surface, whereas tight binding or a large particle/protein surface area may lead to inhibition of protein aggregation. Here we show a clear correlation between the intrinsic protein stability and the nanoparticle effect on the aggregation rate. The results were reached for a series of five mutants of single-chain monellin differing in intrinsic stability toward denaturation, for which a correlation between protein stability and aggregation propensity has been previously documented by Szczepankiewicz et al. [Mol. Biosyst.20107 (2), 521-532]. The aggregation process was monitored by thioflavin T fluorescence in the absence and presence of copolymeric nanoparticles with different hydrophobic characters. For mutants with a high intrinsic stability and low intrinsic aggregation rate, we find that amyloid fibril formation is accelerated by nanoparticles. For mutants with a low intrinsic stability and high intrinsic aggregation rate, we find the opposite--a retardation of amyloid fibril formation by nanoparticles. Moreover, both catalytic and inhibitory effects are most pronounced with the least hydrophobic nanoparticles, which have a larger surface accessibility of hydrogen-bonding groups in the polymer backbone
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| 650 |
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4 |
|a Journal Article
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| 650 |
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4 |
|a Research Support, Non-U.S. Gov't
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7 |
|a Acrylamides
|2 NLM
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| 650 |
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7 |
|a Amyloid
|2 NLM
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| 650 |
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7 |
|a Benzothiazoles
|2 NLM
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| 650 |
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7 |
|a Plant Proteins
|2 NLM
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| 650 |
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7 |
|a Thiazoles
|2 NLM
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| 650 |
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7 |
|a Vinyl Compounds
|2 NLM
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| 650 |
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7 |
|a monellin protein, Dioscoreophyllum cumminsii
|2 NLM
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| 650 |
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7 |
|a thioflavin T
|2 NLM
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| 650 |
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7 |
|a 2390-54-7
|2 NLM
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| 650 |
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7 |
|a tert-butylacrylamide
|2 NLM
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| 650 |
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7 |
|a XJ13FSH48K
|2 NLM
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| 700 |
1 |
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|a Szczepankiewicz, O
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Linse, S
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 28(2012), 3 vom: 24. Jan., Seite 1852-7
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
8 |
|g volume:28
|g year:2012
|g number:3
|g day:24
|g month:01
|g pages:1852-7
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| 856 |
4 |
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|u http://dx.doi.org/10.1021/la203078w
|3 Volltext
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