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Título: | Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
Autor: | Castellanos, Milagros; Torres-Pardo, Almudena; Rodríguez-Pérez, Rosa; Gasset, M. CSIC ORCID | Fecha de publicación: | 20-mar-2018 | Editor: | Multidisciplinary Digital Publishing Institute | Citación: | Biomolecules 8(1): 13 (2018) | Resumen: | 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. | Versión del editor: | http://doi.org/10.3390/biom8010013 | URI: | http://hdl.handle.net/10261/162730 | DOI: | 10.3390/biom8010013 | E-ISSN: | 2218-273X |
Aparece en las colecciones: | (IQF) Artículos |
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biomolecules-08-00013.pdf | 6,66 MB | Adobe PDF | Visualizar/Abrir |
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