Amyloid assembly endows gad m 1 with biomineralization properties
Acid proteins capable of nucleating Ca 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-binding motifs in proteins. Calcium is bound by the loop region. These motifs are found in many proteins t...
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ftcsic:oai:digital.csic.es:10261/180755 2023-05-15T15:27:29+02:00 Amyloid assembly endows gad m 1 with biomineralization properties Castellanos, M. Torres-Pardo, A. Rodríguez-Pérez, R. Gasset, M. 2018 http://hdl.handle.net/10261/180755 https://doi.org/10.3390/biom8010013 eng eng doi:10.3390/biom8010013 issn: 2218-273X http://hdl.handle.net/10261/180755 openAccess##Artículo##Biomolecules 8 (2018)########MINECO/ICTI2013-2016/BFU2015-72271-EXP##amyloids; Gad m 1; EF-hand motif; calcium carbonate precipitation; calcite ######Publisher's version##Sí 2018 ftcsic https://doi.org/10.3390/biom8010013 2019-04-30T23:22:22Z Acid proteins capable of nucleating Ca 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-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 Ca buffer in fish muscle; the neutral and acid apo-forms of this protein can form amyloids. Since Ca-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. Peer Reviewed Other/Unknown Material atlantic cod Digital.CSIC (Spanish National Research Council) Biomolecules 8 1 13 |
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Open Polar |
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Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
English |
description |
Acid proteins capable of nucleating Ca 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-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 Ca buffer in fish muscle; the neutral and acid apo-forms of this protein can form amyloids. Since Ca-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. Peer Reviewed |
author |
Castellanos, M. Torres-Pardo, A. Rodríguez-Pérez, R. Gasset, M. |
spellingShingle |
Castellanos, M. Torres-Pardo, A. Rodríguez-Pérez, R. Gasset, M. Amyloid assembly endows gad m 1 with biomineralization properties |
author_facet |
Castellanos, M. Torres-Pardo, A. Rodríguez-Pérez, R. Gasset, M. |
author_sort |
Castellanos, M. |
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 |
publishDate |
2018 |
url |
http://hdl.handle.net/10261/180755 https://doi.org/10.3390/biom8010013 |
genre |
atlantic cod |
genre_facet |
atlantic cod |
op_relation |
doi:10.3390/biom8010013 issn: 2218-273X http://hdl.handle.net/10261/180755 |
op_rights |
openAccess##Artículo##Biomolecules 8 (2018)########MINECO/ICTI2013-2016/BFU2015-72271-EXP##amyloids; Gad m 1; EF-hand motif; calcium carbonate precipitation; calcite ######Publisher's version##Sí |
op_doi |
https://doi.org/10.3390/biom8010013 |
container_title |
Biomolecules |
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8 |
container_issue |
1 |
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13 |
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1766357919847153664 |