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231225s2019 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.9b01420
|2 doi
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|a pubmed25n0998.xml
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|a (DE-627)NLM299469794
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|a (NLM)31334660
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Criado-Gonzalez, Miryam
|e verfasserin
|4 aut
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| 245 |
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|a Phase Separation in Supramolecular Hydrogels Based on Peptide Self-Assembly from Enzyme-Coated Nanoparticles
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|c 2019
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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
|b cr
|2 rdacarrier
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|a Date Completed 13.08.2020
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|a Date Revised 13.08.2020
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Spatial localization of biocatalysts, such as enzymes, has recently proven to be an effective process to direct supramolecular self-assemblies in a spatiotemporal way. In this work, silica nanoparticles (NPs) functionalized covalently by alkaline phosphatase (NPsAP) induce the localized growth of self-assembled peptide nanofibers from NPs by dephosphorylation of Fmoc-FFpY peptides (Fmoc: fluorenylmethyloxycarbonyl; F: phenylalanine; Y: tyrosine; p: phosphate group). The fibrillary nanoarchitecture around NPs@AP underpins a homogeneous hydrogel, which unexpectedly undergoes a macroscopic shape change over time. This macroscopic change is due to a phase separation leading to a dense phase (in NPs and nanofibers) in the center of the vial and surrounded by a dilute one, which still contains NPs and peptide self-assemblies. We thus hypothesize that the phase separation is not a syneresis process. Such a change is only observed when the enzymes are localized on the NPs. The dense phase contracts with time until reaching a constant volume after several days. For a given phosphorylated peptide concentration, the dense phase contracts faster when the NPs@AP concentration is increased. For a given NPs@AP concentration, it condenses faster when the peptide concentration increases. We hypothesize that the appearance of a dense phase is not only due to attractive interactions between NPs@AP but also to the strong interactions of self-assembled peptide nanofibers with the enzymes, covalently fixed on the NPs
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Coated Materials, Biocompatible
|2 NLM
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|a Hydrogels
|2 NLM
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|a Peptides
|2 NLM
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|a Silicon Dioxide
|2 NLM
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|a 7631-86-9
|2 NLM
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|a Alkaline Phosphatase
|2 NLM
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|a EC 3.1.3.1
|2 NLM
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|a Fores, Jennifer Rodon
|e verfasserin
|4 aut
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|a Carvalho, Alain
|e verfasserin
|4 aut
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|a Blanck, Christian
|e verfasserin
|4 aut
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|a Schmutz, Marc
|e verfasserin
|4 aut
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|a Kocgozlu, Leyla
|e verfasserin
|4 aut
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|a Schaaf, Pierre
|e verfasserin
|4 aut
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|a Jierry, Loïc
|e verfasserin
|4 aut
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|a Boulmedais, Fouzia
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1985
|g 35(2019), 33 vom: 20. Aug., Seite 10838-10845
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnas
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| 773 |
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|g volume:35
|g year:2019
|g number:33
|g day:20
|g month:08
|g pages:10838-10845
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|u http://dx.doi.org/10.1021/acs.langmuir.9b01420
|3 Volltext
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