Amyloid Assembly Endows Gad m 1 with Biomineralization Properties
AbstractAcid proteins capable of nucleating Ca2+ and displaying aggregation capacity play key roles in the formation of calcium carbonate biominerals. The helix-loop helix EF-hands are the most common Ca2+-binding motifs in proteins. Calcium is bound by the loop region. These motifs are found in many proteins that are regulated by calcium. Gad m 1, an Atlantic cod β-parvalbumin isoform, is a monomeric EF-hand protein that acts as a Ca2+ buffer in fish muscle; the neutral and acid apo-forms of this protein can form amyloids. Since Ca2+-nucleating proteins have a propensity to form extended β-strand structures, we wondered whether amyloid assemblies of an EF-hand protein were able to influence calcium carbonate crystallization in vitro. Here, we used the Gad m 1 chain as a model to generate monomeric and amyloid assemblies and to analyze their effect on calcite formation in vitro. We found that only amyloid assemblies alter calcite morphology. View Full-Text
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Castellanos, M.; Torres-Pardo, A.; Rodríguez-Pérez, R.; Gasset, M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules 2018, 8, 13.
Castellanos M, Torres-Pardo A, Rodríguez-Pérez R, Gasset M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules. 2018; 8(1):13.Chicago/Turabian Style
Castellanos, Milagros; Torres-Pardo, Almudena; Rodríguez-Pérez, Rosa; Gasset, María. 2018. "Amyloid Assembly Endows Gad m 1 with Biomineralization Properties." Biomolecules 8, no. 1: 13.
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