ArticleACS applied materials & interfaces2025
Host-Gated Enzymatic Release (H-GER) Enables Colorimetric Transduction for Enzyme Measurement.
Article in ACS applied materials & interfaces, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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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Who cites it
1 citing paper in PubMed.
- Protease-Triggered Chromogenic Release From Peptide-Modified Calcium Carbonate Microspheres Enables Colorimetric Detection of Porphyromonas gingivalis Activity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
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Authors and funding
9 authors.
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Abstract
We introduce Host-Gated Enzymatic Release (H-GER) as an alternative colorimetric signal transduction mechanism for measuring amylase activity. This assay uses a visually colored complex formed when hydroxypropyl-γ-cyclodextrin (HP-γ-CD) binds to the aggregachromic dye CRANAD-2, with the HP side chains playing a key role in the complexation. The analytical capability of this visually addressable assay relies on changes in dye dispersity, triggered by the enzymatic release of gated CRANAD-2 from HP-γ-CD host. Upon cleavage of HP-γ-CD, the freed dye clusters in the aqueous environment, resulting in a sequence of color changes observed by the naked eye. The H-GER assay demonstrated a limit of detection of 154 U/mL for α-amylase. Analysis based on Michaelis-Menten kinetics and molecular dynamics simulations revealed that the H-GER assay exhibits good enzymatic specificity, despite showing reduced catalytic efficiency. These results demonstrate that H-GER is an effective and potentially valuable signal transduction mechanism that expands the current toolbox for developing
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