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The authors looked at developing a PMMA nanoparticle fabric dye that would be more sustainable compared to traditional fabric dyes. They were able to create PMMA based dyes in different colors that were also durable (i.e., did not fade quickly on fabric).

As fast fashion explodes in popularity, the fashion industry remains one of the most prominent industries responsible for pollution. This pollution includes a lack of treatment for textile dyes that remain toxic or carcinogenic as they persist in wastewater. To resolve this, the authors of this study set out to determine the efficacy of using edible white rot fungi for cell-based biodegradation of textile dyes into harmless chemicals. This method takes advantage of fungi found in excess from the fungi industry, decreasing food waste while addressing textile waste in tandem.

Dye-sensitized solar cells (DSSC) use dye as the photoactive material, which capture the incoming photon of light and use the energy to excite electrons. Research in DSSCs has centered around improving the efficacy of photosensitive dyes. A fruit's color is defined by a unique set of molecules, known as a pigment profile, which changes as a fruit progresses from ripe to rotten. This project investigates the use of fresh and rotten fruit extracts as the photoactive dye in a DSSC.

Optical reporters like tetrazolium dyes, exemplified by 5-diphenyl tetrazolium bromide (MTT), are effective tools for quantifying cellular responses under experimental conditions. These dyes assess cell viability by producing brightly-colored formazan dyes when reduced inside active cells. However, certain small molecules, including reducing agents like ascorbic acid, cysteine, and glutathione (GSH), can interfere with MTT assays, potentially compromising accuracy.

Here, seeking to better understand the effects of gadolinium-based contrast agents, dyes typically used for MRI scans, the authors evaluated the activity of catalase found in beef liver both with and without gadodiamide when exposed to hydrogen peroxide. They found that gadioamide did not significantly inhibit catalase's activity, attributing this lack of effects to the chelating agent found in gadodiamide.