Publications by authors named "Emily Manderfeld"

Biofouling is a major challenge for sustainable shipping, filter membranes, heat exchangers, and medical devices. The development of fouling-resistant coatings requires the evaluation of their effectiveness. Such an evaluation is usually based on the assessment of fouling progression after different exposure times to the target medium (e.

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Biofouling on surfaces in contact with sea- or brackish water can severely impact the function of devices like reverse osmosis modules. Single species laboratory assays are frequently used to test new low fouling materials. The choice of bacterial strain is guided by the natural population present in the application of interest and decides on the predictive power of the results.

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Membrane separation processes including reverse osmosis are now considered essential techniques for water and wastewater treatment, especially in water-scarce areas where desalination and water reuse can augment the water supply. However, biofouling remains a significant challenge for these processes and in general for marine biological fouling, which results in increased energy consumption and high operational costs. Especially in flat sheet membrane modules, intense biofilm growth occurs on the feed spacer at points of contact to the membrane surface.

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Dendritic polyglycerol (PG) was covalently coupled to 2-hydroxyethyl methacrylate (HEMA) by an anionically catalyzed ring-opening polymerization generating a dendritic PG-HEMA with four PG repetition units (PGMA). Coatings of the methacrylate monomer were prepared by grafting-through and compared against commercially available hydrophilic monomers of HEMA, poly(ethylene) glycol methacrylate (PEGMA), and poly(propylene) glycol methacrylate (PPGMA). The obtained coatings were characterized by modern surface analytical techniques, including water contact angle goniometry (sessile and captive bubble), attenuated total internal reflection Fourier transform infrared spectroscopy, and atomic force microscopy.

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In cells, proteins are embedded in a crowded environment that controls their properties via manifold avenues including weak protein-macromolecule interactions. A molecular level understanding of these quinary interactions and their contribution to protein stability, function, and localization in the cell is central to modern structural biology. Using a mutational analysis to quantify the energetic contributions of single amino acids to the stability of the ALS related protein superoxide dismutase I (SOD1) in mammalian cells, we show that quinary interactions destabilize SOD1 by a similar energetic offset for most of the mutants, but there are notable exceptions: Mutants that alter its surface properties can even lead to a stabilization of the protein in the cell as compared to the test tube.

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