ArticleArchives of oral biology2025
Ameloblastin binding to biomimetic models of cell membranes - A continuum of intrinsic disorder.
Article in Archives of oral biology, 2025. 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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3 authors.
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Abstract
objectiveA 37-residue amino acid sequence corresponding to the segment encoded by exon-5 of murine ameloblastin (Ambn), AB2 (Y67-Q103), has been implicated with membrane association, ameloblastin self-assembly, and amelogenin-binding. Our aim was to characterize, at the residue level, the structural behavior of AB2 bound to chemical mimics of biological membranes using NMR spectroscopy.
designTo better define the structure of AB2 using NMR-based methods, recombinant
resultsAmide chemical shift and intensity perturbations observed in
conclusionsA continuum of intrinsic disorder in the membrane-bound state may be responsible for ameloblastin's ability to dynamically interact with multiple partners at the same site during amelogenesis.
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