Castellanos, M.; Torres-Pardo, A.; Rodríguez-Pérez, R.; Gasset, M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules2018, 8, 13.
Castellanos, M.; Torres-Pardo, A.; Rodríguez-Pérez, R.; Gasset, M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules 2018, 8, 13.
Castellanos, M.; Torres-Pardo, A.; Rodríguez-Pérez, R.; Gasset, M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules2018, 8, 13.
Castellanos, M.; Torres-Pardo, A.; Rodríguez-Pérez, R.; Gasset, M. Amyloid Assembly Endows Gad m 1 with Biomineralization Properties. Biomolecules 2018, 8, 13.
Abstract
Acid proteins capable of nucleating Ca2+ and displaying aggregation capacity play key roles in the formation of calcium carbonate biominerals. EF-hands are among the largest Ca2+-binding motif in proteins. Gad m 1, an Atlantic cod β-parvalbumin isoform, is a monomeric EF-hand protein that acts as a Ca2+ buffer in fish muscle and is able to form amyloids under acidic conditions. Since nucleating Ca2+ protein have a propensity to form extended β-strand structures, we wondered whether amyloid assemblies of a protein containing refolded EF-hand motifs were able to influence the in vitro calcium carbonate crystallization. Here we have used the Gad m 1 chain as model to generate monomeric and amyloid assemblies and analyze their effect on in vitro calcite formation. We found that only amyloid assemblies alter calcite morphology.
Keywords
amyloids; Gad m 1, EF-hand motif, calcium carbonate precipitation, calcite
Subject
Chemistry and Materials Science, Biomaterials
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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