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- ItemPrecise AuxPt1-x Alloy Nanoparticle Array of Tunable Composition for Catalytic Applications([London] : Macmillan Publishers Limited, part of Springer Nature, 2016) Jahn, Sarah; Lechner, Sebastian J.; Freichels, Helene; Möller, Martin; Spatz, Joachim P.A 3-dimensional Block Copolymer Micellar nanoLithography (BCML) process was used to prepare AuxPt1−x alloy nanoparticles (NPs) monodisperse in size and composition, strongly anchored onto SiO2-particles (0.2 wt.% AuxPt1−x/SiO2). The particles possess a face-centered cubic (fcc) crystal structure and their size could be varied from 3–12 nm. We demonstrate the uniformity of the Au/Pt composition by analyzing individual NPs by energy-dispersive X-ray spectroscopy. The strongly bound AuxPt1−x NPs catalyzed the oxidation of CO with high activity. Thermal ageing experiments in pure CO2 as well as in ambient atmosphere demonstrated stability of the size distribution for times as long as 22 h.
- ItemFibronectin promotes directional persistence in fibroblast migration through interactions with both its cell-binding and heparin-binding domains([London] : Macmillan Publishers Limited, part of Springer Nature, 2017) Missirlis, Dimitris; Haraszti, Tamás; Kessler, Horst; Spatz, Joachim P.The precise mechanisms through which insoluble, cell-adhesive ligands induce and regulate directional cell migration remain obscure. We recently demonstrated that elevated surface density of physically adsorbed plasma fibronectin (FN) promotes high directional persistence in fibroblast migration. While cell-FN association through integrins α5β1 and αvβ3 was necessary, substrates that selectively engaged these integrins did not support the phenotype. We here show that high directional persistence necessitates a combination of the cell-binding and C-terminal heparin-binding domains of FN, but does not require the engagement of syndecan-4 or integrin α4β1. FN treatment with various fixation agents indicated that associated changes in fibroblast motility were due to biochemical changes, rather than alterations in its physical state. The nature of the coating determined the ability of fibroblasts to assemble endogenous or exogenous FN, while FN fibrillogenesis played a minor, but significant, role in regulating directionality. Interestingly, knockdown of cellular FN abolished cell motility altogether, demonstrating a requirement for intracellular processes in enabling fibroblast migration on FN. Lastly, kinase inhibition experiments revealed that regulation of cell speed and directional persistence are decoupled. Hence, we have identified factors that render full-length FN a promoter of directional migration and discuss the possible, relevant mechanisms.