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Open AccessArticle

Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

IMDEA Nanoscience, 28049 Madrid, Spain
Departamento de Química Inorgánica, Facultad de Químicas, Universidad Complutense, 28040 Madrid, Spain
Instituto de Investigación Hospital Universitario La Paz (IdiPaz), 28046 Madrid, Spain
Instituto Química-Física “Rocasolano”, Consejo Superior de Investigaciones Científicas, 28006 Madrid, Spain
Author to whom correspondence should be addressed.
Biomolecules 2018, 8(1), 13;
Received: 18 January 2018 / Revised: 2 March 2018 / Accepted: 16 March 2018 / Published: 20 March 2018
(This article belongs to the Special Issue Functional Amyloids)
Acid 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
Keywords: amyloids; Gad m 1; EF-hand motif; calcium carbonate precipitation; calcite amyloids; Gad m 1; EF-hand motif; calcium carbonate precipitation; calcite
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MDPI and ACS Style

Castellanos, M.; Torres-Pardo, A.; Rodríguez-Pérez, R.; Gasset, M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules 2018, 8, 13.

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