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Minor chemistry changes alter surface hydration to control fibronectin adsorption and assembly into nanofibrils

Research output: Contribution to journalArticle

Mateusz Krzysztof Bieniek, Virginia Llopis-Hernandez, Katie Douglas, Manuel Salmeron-Sanchez, Christian Lorenz

Original languageEnglish
Article number1900169
Pages (from-to)1-13
Issue number12
Early online date28 Oct 2019
Accepted/In press30 Sep 2019
E-pub ahead of print28 Oct 2019
PublishedDec 2019


King's Authors


Fibronectin (FN) is a large glycoprotein which links and transmits signals between the cell’s cytoskeleton and the extracellular matrix. FN organisation into fibrils and then fibrillogenesis can be induced with the right substrate, such as poly(ethyl acrylate) (PEA), on which FN becomes extended. Interestingly, the almost identical polymer poly(methyl acrylate) (PMA), which has one less methylene bridge (-CH2-), doesn’t cause fibrillogenesis. To investigate the difference in FN behaviour on PEA and PMA, we model the two substrates using EA and MA functionalised self-assembled monolayers (SAMs). We confirm experimentally that the EA and MA SAMs exhibit a similar behaviour in vitro to the polymers in terms of fibronectin fibrillogenesis, domain exposure and cell adhesion. Our all-atom molecular dynamics simulations of the FNIII 9-10 domains interacting with each SAM show the adsorption of these two domains on EA SAMs and no adsorption on MA SAMs. Consistently, the experiments show that FN fibrillogenesis takes place on EA SAMs but not on MA SAMs. We found that the extra methylene group in the EA headgroup leads to more motion within the headgroup that results in a markedly less dense hydration layer, which allows FN to adsorb to the substrate and therefore facilitates FN fibrillogenesis

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