ArticleInternational journal of biological macromolecules2026
Marine sulfated glycan inhibits tau-heparan sulfate interaction and tau cellular uptake.
Article in International journal of biological macromolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Heparan sulfate (HS) proteoglycans mediate the cellular uptake of tau, a critical step in the prion-like spread of tau pathology in Alzheimer's disease. In this study, we tested if several marine sulfated glycan of diverse structures can inhibit the tau-HS interaction. Through experiments of SPR we found that marine-derived sulfated fucans bind tau with similar affinity to heparin, whereas fucosylated chondroitin sulfates (FucCS) from several holothurian species bind tau with substantially higher affinity. Using solution NMR, we further characterized FucCS-tau interactions with residue-level resolution, revealing complex binding behavior distinct from heparin-tau binding. A high-affinity site is observed as peak intensity loss spanning the middle of PRR2 through R' of tau at low FucCS concentration, whereas another weaker binding site is characterized by both chemical shift perturbation and gradual peak intensity attenuation from the end of N2 through the middle of PRR2. Finally, we demonstrated that FucCSs inhibit tau uptake in SH-SY5Y cells with an IC
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