Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

作者：Castellanos Milagros; Torres Pardo Almudena; Rodriguez Perez Rosa; Gasset Maria^*

来源：Biomolecules, 2018, 8(1): 13.

DOI：10.3390/biom8010013

• amyloids
• Gad m 1
• EF-hand motif
• calcium carbonate precipitation
• calcite

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 Ca-2 +/- -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 beta-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 Ca-2 +/- -nucleating proteins have a propensity to form extended beta-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.

• 出版日期2018-3