Publications by authors named "Miryeong Yoo"

Article Synopsis
  • Prions are misfolded proteins that cause prion diseases by forming amyloids, which disrupt brain function and convert normal proteins into their harmful forms.
  • Recent research identified acylthiosemicarbazides as effective inhibitors of prion aggregation, achieving nearly complete inhibition in lab tests.
  • These compounds not only reduce the formation of new prions but also disassemble existing aggregates, showing promise as potential treatments for prion infections.
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Prion diseases are neurodegenerative disorders in humans and animals for which no therapies are currently available. Here, we report that Valeton (Zingiberaceae) () extract was partly effective in decreasing prion aggregation and propagation in both in vitro and in vivo models. extract inhibited self-aggregation of recombinant prion protein (PrP) in a test tube assay and decreased the accumulation of scrapie PrP (PrP) in ScN2a cells, a cultured neuroblastoma cell line with chronic prion infection, in a concentration-dependent manner.

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Self-assembling peptides are biomedical materials with unique structures that are formed in response to various environmental conditions. Governed by their physicochemical characteristics, the peptides can form a variety of structures with greater reactivity than conventional non-biological materials. The structural divergence of self-assembling peptides allows for various functional possibilities; when assembled, they can be used as scaffolds for cell and tissue regeneration, and vehicles for drug delivery, conferring controlled release, stability, and targeting, and avoiding side effects of drugs.

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