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Title

Amyloid Assembly Endows Gad m 1 with Biomineralization Properties

AuthorsCastellanos, Milagros; Torres-Pardo, Almudena; Rodríguez-Pérez, Rosa; Gasset, M. CSIC ORCID
Issue Date20-Mar-2018
PublisherMultidisciplinary Digital Publishing Institute
CitationBiomolecules 8(1): 13 (2018)
AbstractAcid 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.
Publisher version (URL)http://doi.org/10.3390/biom8010013
URIhttp://hdl.handle.net/10261/162730
DOI10.3390/biom8010013
E-ISSN2218-273X
Appears in Collections:(IQFR) Artículos

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