Castellanos, MilagrosTorres Pardo, María De La AlmudenaRodríguez Pérez, RosaGasset, María2023-06-172023-06-172018-03-20Castellanos, M., Torres Pardo, M. A., Rodríguez Pérez, R. & Gasset, M. «Amyloid Assembly Endows Gad m 1 with Biomineralization Properties». Biomolecules, vol. 8, n.o 1, marzo de 2018, p. 13. DOI.org (Crossref), https://doi.org/10.3390/biom8010013.2218-273X10.3390/biom8010013https://hdl.handle.net/20.500.14352/12589Acid 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.engAtribución 3.0 Españahttps://creativecommons.org/licenses/by/3.0/es/journal articlehttps://doi.org/10.3390/biom8010013https://www.mdpi.com/2218-273X/8/1/13open accessAmyloidsGad m 1EF-hand motifCalcium carbonate precipitationCalciteQuímica inorgánica (Química)2303 Química Inorgánica