Amyloid Assembly Endows Gad m 1 with Biomineralization Properties
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 protei...
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Multidisciplinary Digital Publishing Institute
2018
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Online Access: | https://doi.org/10.3390/biom8010013 |
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ftmdpi:oai:mdpi.com:/2218-273X/8/1/13/ 2023-08-20T04:05:11+02:00 Amyloid Assembly Endows Gad m 1 with Biomineralization Properties Milagros Castellanos Almudena Torres-Pardo Rosa Rodríguez-Pérez María Gasset agris 2018-03-20 application/pdf https://doi.org/10.3390/biom8010013 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/biom8010013 https://creativecommons.org/licenses/by/4.0/ Biomolecules; Volume 8; Issue 1; Pages: 13 amyloids Gad m 1 EF-hand motif calcium carbonate precipitation calcite Text 2018 ftmdpi https://doi.org/10.3390/biom8010013 2023-07-31T21:26:18Z 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. Text atlantic cod MDPI Open Access Publishing Biomolecules 8 1 13 |
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MDPI Open Access Publishing |
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English |
topic |
amyloids Gad m 1 EF-hand motif calcium carbonate precipitation calcite |
spellingShingle |
amyloids Gad m 1 EF-hand motif calcium carbonate precipitation calcite Milagros Castellanos Almudena Torres-Pardo Rosa Rodríguez-Pérez María Gasset Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
topic_facet |
amyloids Gad m 1 EF-hand motif calcium carbonate precipitation calcite |
description |
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. |
format |
Text |
author |
Milagros Castellanos Almudena Torres-Pardo Rosa Rodríguez-Pérez María Gasset |
author_facet |
Milagros Castellanos Almudena Torres-Pardo Rosa Rodríguez-Pérez María Gasset |
author_sort |
Milagros Castellanos |
title |
Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
title_short |
Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
title_full |
Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
title_fullStr |
Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
title_full_unstemmed |
Amyloid Assembly Endows Gad m 1 with Biomineralization Properties |
title_sort |
amyloid assembly endows gad m 1 with biomineralization properties |
publisher |
Multidisciplinary Digital Publishing Institute |
publishDate |
2018 |
url |
https://doi.org/10.3390/biom8010013 |
op_coverage |
agris |
genre |
atlantic cod |
genre_facet |
atlantic cod |
op_source |
Biomolecules; Volume 8; Issue 1; Pages: 13 |
op_relation |
https://dx.doi.org/10.3390/biom8010013 |
op_rights |
https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.3390/biom8010013 |
container_title |
Biomolecules |
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8 |
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1 |
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13 |
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1774715659034296320 |