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Self-stabilized fibronectin films at the air/water interface

Published online by Cambridge University Press:  04 November 2019

Thanga Bhuvanesh ,
Rainhard Machatschek ,
Yue Liu ,
Nan Ma  and
Andreas Lendlein
Thanga Bhuvanesh
Affiliation:
Institute of Biomaterial Research and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24/25, 14476 Potsdam, Germany
Rainhard Machatschek
Affiliation:
Institute of Biomaterial Research and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany
Yue Liu
Affiliation:
Institute of Biomaterial Research and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24/25, 14476 Potsdam, Germany
Nan Ma
Affiliation:
Institute of Biomaterial Research and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany
Andreas Lendlein*
Affiliation:
Institute of Biomaterial Research and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstrasse 55, 14513 Teltow, Germany Institute of Chemistry, University of Potsdam, Karl-Liebknecht-Str. 24/25, 14476 Potsdam, Germany Institute of Chemistry and Biochemistry, Freie Universität Berlin, 14195 Berlin, Germany
*
*(Email: lendlein@uni-potsdam.de)
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Abstract

Fibronectin (FN) is a mediator molecule, which can connect cell receptors to the extracellular matrix (ECM) in tissues. This function is highly desirable for biomaterial surfaces in order to support cell adhesion. Controlling the fibronectin adsorption profile on substrates is challenging because of possible conformational changes after deposition, or due to displacement by secondary proteins from the culture medium. Here, we aim to develop a method to realize self-stabilized ECM glycoprotein layers with preserved native secondary structure on substrates. Our concept is the assembly of FN layers at the air-water (A-W) interface by spreading FN solution as droplets on the interface and transfer of the layer by the Langmuir-Schäfer (LS) method onto a substrate. It is hypothesized that 2D confinement and high local concentration at A-W interface supports FN self-interlinking to form cohesive films. Rising surface pressure with time, plateauing at 10.5 mN·m-1 (after 10 hrs), indicated that FN was self-assembling at the A-W interface. In situ polarization-modulation infrared reflection absorption spectroscopy of the layer revealed that FN maintained its native anti-parallel β-sheet structure after adsorption at the A-W interface. FN self-interlinking and elasticity was shown by the increase in elastic modulus and loss modulus with time using interfacial rheology. A network-like structure of FN films formed at the A-W interface was confirmed by atomic force microscopy after LS transfer onto Si-wafer. FN films consisted of native, globular FN molecules self-stabilized by intermolecular interactions at the A-W interface. Therefore, the facile FN self-stabilized network-like films with native anti-parallel β-sheet structure produced here, could serve as stable ECM protein coatings to enhance cell attachment on in vitro cell culture substrates and planar implant materials.

Keywords

thin filminfrared (IR) spectroscopybiomimetic (assembly)biomaterial
Type
Articles
Information
MRS Advances , Volume 5 , Issue 12-13: Soft Materials and Biomaterials , 2020 , pp. 609 - 620
Copyright
Copyright © Materials Research Society 2019

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