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231225s2021 xx |||||o 00| ||eng c |
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|a 10.1002/adma.202104187
|2 doi
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|a pubmed24n1483.xml
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|a eng
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| 100 |
1 |
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|a Chen, Mengmeng
|e verfasserin
|4 aut
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| 245 |
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|a Crack Suppression in Conductive Film by Amyloid-Like Protein Aggregation toward Flexible Device
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|c 2021
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 24.07.2024
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|a Date Revised 26.07.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a © 2021 Wiley-VCH GmbH.
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|a A fatal weakness in flexible electronics is the mechanical fracture that occurs during repetitive fatigue deformation; thus, controlling the crack development of the conductive layer is of prime importance and has remained a great challenge until now. Herein, this issue is tackled by utilizing an amyloid/polysaccharide molecular composite as an interfacial binder. Sodium alginate (SA) can take part in amyloid-like aggregation of the lysozyme, leading to the facile synthesis of a 2D protein/saccharide hybrid nanofilm over an ultralarge area (e.g., >400 cm2 ). The introduction of SA into amyloid-like aggregates significantly enhances the mechanical strength of the hybrid nanofilm, which, with the help of amyloid-mediated interfacial adhesion, effectively diminishes the microcracks in the hybrid nanofilm coating after repetitive bending or stretching. The microcrack-free hybrid nanofilm then shows high interfacial activity to induce electroless deposition of metal in a Kelvin model on a substrate, which noticeably suppresses the formation of microcracks and consequent conductivity loss during the bending and stretching of the metal-coated flexible substrates. This work underlines the significance of amyloid/polysaccharide nanocomposites in the design of interfacial binders for reliable flexible electronic devices and represents an important contribution to mimicking amyloid and polysaccharide-based adhesive cements created by organisms
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|a Journal Article
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|a amyloid
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|a flexible electronics
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|a nanofilms
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|a protein assembly
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|a surface modification
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|a Alginates
|2 NLM
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|a Muramidase
|2 NLM
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| 650 |
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|a EC 3.2.1.17
|2 NLM
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| 650 |
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|a Protein Aggregates
|2 NLM
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| 650 |
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|a Amyloid
|2 NLM
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| 650 |
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|a Amyloidogenic Proteins
|2 NLM
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| 700 |
1 |
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|a Yang, Facui
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Chen, Xi
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Qin, Rongrong
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Pi, Hemu
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Zhou, Guijiang
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yang, Peng
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Advanced materials (Deerfield Beach, Fla.)
|d 1998
|g 33(2021), 44 vom: 15. Nov., Seite e2104187
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|x 1521-4095
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|g volume:33
|g year:2021
|g number:44
|g day:15
|g month:11
|g pages:e2104187
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|u http://dx.doi.org/10.1002/adma.202104187
|3 Volltext
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