ArticleBMC research notes2026
Tagged and untagged amyloid precursor protein E2 domain have comparable thermal stability and metal-ion binding propensity.
Article in BMC research notes, 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
5 authors.
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Abstract
objectiveThe amyloid precursor protein, central to the pathology of several disease including Alzheimer's disease, cancer and obesity, represents a therapeutic target. Being able to screen amyloid precursor protein, and its domains, in rapid high-throughput assays could advance drug discovery efforts. The purpose of this study was to determine if removal of a C-terminal tag from the amyloid precursor protein E2 domain was necessary for ligand screening using differential scanning fluorometry. To this end, we assessed both the thermal stability and metal-ion binding propensity in both the tagged and untagged protein.
resultsThe C-terminal myc-6xHis-tag does not impact the amyloid precursor protein E2 domain thermal stability with comparable melting temperatures of 59.4 °C and 59.1 °C in sodium phosphate buffer, for tagged and untagged protein, respectively. Additionally, the tag had no influence on the ability of the metal-ions, Zn
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