Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

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Castellanos, Milagros and Torres Pardo, Almudena and Rodríguez-Pérez, Rosa and Gasset, María (2018) Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules, 8 (1). p. 13. ISSN 2218-273X

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Official URL: https://doi.org/10.3390/biom8010013




Abstract

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.


Item Type:Article
Uncontrolled Keywords:amyloids; Gad m 1; EF-hand motif; calcium carbonate precipitation; calcite
Subjects:Sciences > Chemistry > Chemistry, Inorganic
ID Code:66138
Deposited On:17 Jun 2021 13:55
Last Modified:18 Jun 2021 07:16

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