ArticleFrontiers in chemistry2026
Topology- and sequence-controlled β-amyloid recognition by a KLVFF/transferrin-functionalized csq porphyrinic zirconium MOF (PCN-222).
Article in Frontiers in chemistry, 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
Recognition of amyloid-β (Aβ) by structurally defined inorganic scaffolds offers a route to dissecting how framework geometry and surface chemistry govern peptide-material interactions. We report transferrin (Tf)/KLVFF-PCN-222, a bioinorganic recognition platform built by covalently co-grafting the Aβ-homologous pentapeptide KLVFF and transferrin (Tf) onto the csq-topology porphyrinic zirconium MOF PCN-222 via EDC/NHS chemistry. The one-dimensional hexagonal mesopore channels (∼3.7 nm) and the dense meso-tetrakis (4-carboxyphenyl)porphyrin (TCPP) sites of the csq framework provide geometric access for Aβ1-42 monomer diffusion and an array of peptide-porphyrin recognition contacts. Fluorescence quenching and isothermal titration calorimetry returned an apparent dissociation constant (
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