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  4. Temperature-Controlled Masking/Unmasking of Cell-Adhesive Cues with Poly(ethylene glycol) Methacrylate Based Brushes
 
research article

Temperature-Controlled Masking/Unmasking of Cell-Adhesive Cues with Poly(ethylene glycol) Methacrylate Based Brushes

Desseaux, Solenne  
•
Klok, Harm-Anton  
2014
Biomacromolecules

Thin, thermoresponsive polymer coatings that allow to reversibly modulate cell adhesion and detachment are attractive substrates for cell sheet engineering. Usually, this is accomplished by applying thin poly(N-isopropylacrylamide) (PNIPAM) coatings, which allow cell adhesion via nonspecific interactions above the collapse temperature (TT) of the surface-attached polymer and cell detachment upon cooling below TT. This Article presents an alternative, thermoresponsive polymer platform that is based on 2-(2-methoxyethoxy)ethyl methacrylate (MEO2MA) containing copolymer brushes prepared via surface-initiated atom transfer radical polymerization (SI-ATRP). These brushes are interesting as they gradually collapse and dehydrate upon increasing the temperature from 10 to 40 degrees C, yet resist nonspecific adhesion of cells over this entire temperature window. The MEO2MA based brushes presented here were modified via a two-step postpolymerization modification protocol to introduce cell-adhesive RGD containing peptide ligands. The possibility to reversibly control the swelling and collapse of these brush films by varying temperature allows to modulate the effectively available surface concentration of these cell-adhesive cues and thus provides a way to mask/unmask their biological activity. As a first proof of concept, this Article demonstrates that these MEO2MA brush copolymer films enable integrin-mediated adhesion of 3T3 fibroblasts at 37 degrees C and allow release of these cells by cooling to 23 degrees C. The use of cell-adhesive ligands, which can be thermoreversibly masked/unmasked, is attractive as it enables the use of serum-free cell culture conditions. This is advantageous since it avoids possible concerns regarding eventual toxicity and immunological side effects of serum proteins and also provides opportunities to select for particular cell types and for enhanced control over cell stimulation and differentiation.

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Type
research article
DOI
10.1021/bm501233h
Web of Science ID

WOS:000343026600042

Author(s)
Desseaux, Solenne  
Klok, Harm-Anton  
Date Issued

2014

Publisher

American Chemical Society

Published in
Biomacromolecules
Volume

15

Issue

10

Start page

3859

End page

3865

Editorial or Peer reviewed

REVIEWED

Written at

EPFL

EPFL units
LP  
Available on Infoscience
November 13, 2014
Use this identifier to reference this record
https://infoscience.epfl.ch/handle/20.500.14299/108672
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