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231225s2017 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.7b01532
|2 doi
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|a pubmed24n0914.xml
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|a (DE-627)NLM274242060
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|a (NLM)28749683
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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 |
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|a Vigier-Carrière, Cécile
|e verfasserin
|4 aut
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| 245 |
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|a Control of Surface-Localized, Enzyme-Assisted Self-Assembly of Peptides through Catalyzed Oligomerization
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|c 2017
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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 16.01.2019
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|a Date Revised 16.01.2019
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Localized self-assembly allowing both spatial and temporal control over the assembly process is essential in many biological systems. This can be achieved through localized enzyme-assisted self-assembly (LEASA), also called enzyme-instructed self-assembly, where enzymes present on a substrate catalyze a reaction that transforms noninteracting species into self-assembling ones. Very few LEASA systems have been reported so far, and the control of the self-assembly process through the surface properties represents one essential step toward their use, for example, in artificial cell mimicry. Here, we describe a new type of LEASA system based on α-chymotrypsin adsorbed on a surface, which catalyzes the production of (KL)nOEt oligopeptides from a KLOEt (K: lysine; L: leucine; OEt ethyl ester) solution. When a critical concentration of the formed oligopeptides is reached near the surface, they self-assemble into β-sheets resulting in a fibrillar network localized at the interface that can extend over several micrometers. One significant feature of this process is the existence of a lag time before the self-assembly process starts. We investigate, in particular, the effect of the α-chymotrypsin surface density and KLOEt concentration on the self-assembly kinetics. We find that the lag time can be finely tuned through the surface density in α-chymotrypsin and KLOEt concentration. For a given surface enzyme concentration, a critical KLOEt concentration exists below which no self-assembly takes place. This concentration increases when the surface density in enzyme decreases
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Oligopeptides
|2 NLM
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|a Peptides
|2 NLM
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|a Wagner, Déborah
|e verfasserin
|4 aut
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|a Chaumont, Alain
|e verfasserin
|4 aut
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|a Durr, Baptiste
|e verfasserin
|4 aut
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|a Lupattelli, Paolo
|e verfasserin
|4 aut
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|a Lambour, Christophe
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Schmutz, Marc
|e verfasserin
|4 aut
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| 700 |
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|a Hemmerlé, Joseph
|e verfasserin
|4 aut
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|a Senger, Bernard
|e verfasserin
|4 aut
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|a Schaaf, Pierre
|e verfasserin
|4 aut
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|a Boulmedais, Fouzia
|e verfasserin
|4 aut
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|a Jierry, Loïc
|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 1992
|g 33(2017), 33 vom: 22. Aug., Seite 8267-8276
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:33
|g year:2017
|g number:33
|g day:22
|g month:08
|g pages:8267-8276
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|u http://dx.doi.org/10.1021/acs.langmuir.7b01532
|3 Volltext
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|d 33
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|e 33
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|h 8267-8276
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