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  Polymeric substrates with tunable elasticity and nanoscopically controlled biomolecule presentation

Aydin, D., Louban, I., Perschmann, N., Blümmel, J., Lohmueller, T., Cavalcanti-Adam, E. A., et al. (2010). Polymeric substrates with tunable elasticity and nanoscopically controlled biomolecule presentation. Langmuir, 26(19), 15472-15480. doi:10.1021/la103065x.

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 Urheber:
Aydin, Daniel1, Autor           
Louban, Ilia1, Autor           
Perschmann, Nadine1, 2, Autor           
Blümmel, Jacques1, Autor           
Lohmueller, Theobald1, Autor           
Cavalcanti-Adam, Elisabetta Ada1, 2, Autor           
Haas, Tobias L., Autor
Walczak, Henning, Autor
Kessler, Horst, Autor
Fiammengo, Roberto1, Autor           
Spatz, Joachim P.1, 2, Autor           
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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 Zusammenfassung: Despite tremendous progress in recent years, nanopatterning of hydrated polymeric systems such as hydrogels still represents a major challenge. Here, we employ block copolymer nanolithography to arrange gold nanoparticles on a solid template, followed by the transfer of the pattern to a polymeric hydrogel. In the next step, these nanoparticles serve as specific anchor points for active biomolecules. We demonstrate the engineering of poly(ethylene glycol) hydrogel surfaces with respect to elasticity, nanopatterning, and functionalization with biomolecules. For the first time, biomolecule arrangement on the nanometer scale and substrate stiffness can be varied independently from each other. Young’s moduli, a measure of the compliance of the substrates, can be tuned over 4 orders of magnitude, including the values for all of the different tissues found in the human body. Structured hydrogels can be used to pattern any histidine-tagged protein as exemplified for his-protein A as an acceptor for immunoglobulin. When cell-adhesion-promoting peptide cRGDfK is selectively coupled to gold nanoparticles, the surfaces provide cues for cell−surface interaction and allow for the study of the modulation of cellular adhesion by the mechanical properties of the environment. Therefore, these substrates represent a unique multipurpose platform for studying receptor/ligand interactions with adhering cells, mechanotransduction, and cell-adhesion-dependent signaling.

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Sprache(n): eng - English
 Datum: 2010-08-272010-08-022010-09-132010
 Publikationsstatus: Erschienen
 Seiten: 9
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 510632
DOI: 10.1021/la103065x
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Titel: Langmuir
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Columbus, OH : American Chemical Society
Seiten: - Band / Heft: 26 (19) Artikelnummer: - Start- / Endseite: 15472 - 15480 Identifikator: ISSN: 0743-7463
CoNE: https://pure.mpg.de/cone/journals/resource/954925541194