Control of Enzyme Reactivity in Response to Osmotic Pressure Modulation Mimicking Dynamic Assembly of Intracellular Organelles

© 2023 The Authors. Advanced Materials published by Wiley-VCH GmbH.

Détails bibliographiques
Publié dans:Advanced materials (Deerfield Beach, Fla.). - 1998. - 35(2023), 33 vom: 30. Aug., Seite e2301856
Auteur principal: Schvartzman, Clémence (Auteur)
Autres auteurs: Zhao, Hang, Ibarboure, Emmanuel, Ibrahimova, Vusala, Garanger, Elisabeth, Lecommandoux, Sébastien
Format: Article en ligne
Langue:English
Publié: 2023
Accès à la collection:Advanced materials (Deerfield Beach, Fla.)
Sujets:Journal Article artificial cells elastin-like polypeptides liquid-liquid phase separation microfluidics synthetic organelles Peptides Horseradish Peroxidase EC 1.11.1.- Water 059QF0KO0R
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520 |a © 2023 The Authors. Advanced Materials published by Wiley-VCH GmbH. 
520 |a In response to variations in osmotic stress, in particular to hypertonicity associated with biological dysregulations, cells have developed complex mechanisms to release their excess water, thus avoiding their bursting and death. When water is expelled, cells shrink and concentrate their internal bio(macro)molecular content, inducing the formation of membraneless organelles following a liquid-liquid phase separation (LLPS) mechanism. To mimic this intrinsic property of cells, functional thermo-responsive elastin-like polypeptide (ELP) biomacromolecular conjugates are herein encapsulated into self-assembled lipid vesicles using a microfluidic system, together with polyethylene glycol (PEG) to mimic cells' interior crowded microenvironment. By inducing a hypertonic shock onto the vesicles, expelled water induces a local increase in concentration and a concomitant decrease in the cloud point temperature (Tcp ) of ELP bioconjugates that phase separate and form coacervates mimicking cellular stress-induced membraneless organelle assemblies. Horseradish peroxidase (HRP), as a model enzyme, is bioconjugated to ELPs and is locally confined in coacervates as a response to osmotic stress. This consequently increases local HRP and substrate concentrations and accelerates the kinetics of the enzymatic reaction. These results illustrate a unique way to fine-tune enzymatic reactions dynamically as a response to a physiological change in isothermal conditions 
650 4 |a Journal Article 
650 4 |a artificial cells 
650 4 |a elastin-like polypeptides 
650 4 |a liquid-liquid phase separation 
650 4 |a microfluidics 
650 4 |a synthetic organelles 
650 7 |a Peptides  |2 NLM 
650 7 |a Horseradish Peroxidase  |2 NLM 
650 7 |a EC 1.11.1.-  |2 NLM 
650 7 |a Water  |2 NLM 
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700 1 |a Zhao, Hang  |e verfasserin  |4 aut 
700 1 |a Ibarboure, Emmanuel  |e verfasserin  |4 aut 
700 1 |a Ibrahimova, Vusala  |e verfasserin  |4 aut 
700 1 |a Garanger, Elisabeth  |e verfasserin  |4 aut 
700 1 |a Lecommandoux, Sébastien  |e verfasserin  |4 aut 
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773 1 8 |g volume:35  |g year:2023  |g number:33  |g day:30  |g month:08  |g pages:e2301856 
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