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231225s2018 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.8b00254
|2 doi
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|a pubmed24n0942.xml
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|a (DE-627)NLM282803041
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|a (NLM)29631401
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|a DE-627
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|e rakwb
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|a eng
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|a Li, Xi
|e verfasserin
|4 aut
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|a Bifunctionality of Iminodiacetic Acid-Modified Lysozyme on Inhibiting Zn2+-Mediated Amyloid β-Protein Aggregation
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|c 2018
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|a Date Completed 14.03.2019
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|a Date Revised 14.03.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Aggregation of amyloid β-proteins (Aβ) mediated by metal ions such as Zn2+ has been suggested to be implicated in the progression of Alzheimer's disease (AD). Hence, development of bifunctional agents capable of inhibiting Aβ aggregation and modulating metal-Aβ species is an effective strategy for the treatment of AD. In this work, we modified iminodiacetic acid (IDA) onto human lysozyme (hLys) surface to create an inhibitor of Zn2+-mediated Aβ aggregation and cytotoxicity. The IDA-modified hLys (IDA-hLys) retained the stability and biocompatibility of native hLys. Extensive biophysical and biological analyses indicated that IDA-hLys significantly attenuated Zn2+-mediated Aβ aggregation and cytotoxicity due to its strong binding affinity for Zn2+, whereas native hLys showed little effect. Stopped-flow fluorescence spectroscopy showed that IDA-hLys could protect Aβ from Zn2+-induced aggregation and rapidly depolymerize Zn2+-Aβ aggregates. The research indicates that IDA-hLys is a bifunctional agent capable of inhibiting Aβ fibrillization and modulating Zn2+-mediated Aβ aggregation and cytotoxicity as a strong Zn2+ chelator
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Amyloid beta-Peptides
|2 NLM
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|a Imino Acids
|2 NLM
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|a Muramidase
|2 NLM
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|a EC 3.2.1.17
|2 NLM
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|a Zinc
|2 NLM
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|a J41CSQ7QDS
|2 NLM
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|a iminodiacetic acid
|2 NLM
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|a XQM2L81M8Z
|2 NLM
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1 |
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|a Xie, Baolong
|e verfasserin
|4 aut
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1 |
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|a Dong, Xiaoyan
|e verfasserin
|4 aut
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|a Sun, Yan
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 34(2018), 17 vom: 01. Mai, Seite 5106-5115
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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|g volume:34
|g year:2018
|g number:17
|g day:01
|g month:05
|g pages:5106-5115
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|u http://dx.doi.org/10.1021/acs.langmuir.8b00254
|3 Volltext
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