Preprint Article Version 1 This version is not peer-reviewed

Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

Version 1 : Received: 18 January 2018 / Approved: 18 January 2018 / Online: 18 January 2018 (15:13:24 CET)

A peer-reviewed article of this Preprint also exists.

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. Biomolecules 2018, 8, 13.

Journal reference: Biomolecules 2018, 8, 13
DOI: 10.3390/biom8010013

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.

Subject Areas

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

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