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...
Published in: | Biomolecules |
---|---|
Main Authors: | , , , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
2018
|
Subjects: | |
Online Access: | http://hdl.handle.net/10261/180756 https://doi.org/10.3390/biom8010013 |
id |
ftcsic:oai:digital.csic.es:10261/180756 |
---|---|
record_format |
openpolar |
spelling |
ftcsic:oai:digital.csic.es:10261/180756 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/10261/180756 https://doi.org/10.3390/biom8010013 eng eng MINECO/ICTI2013-2016/BFU2015-72271-EXP Publisher's version Sí doi:10.3390/biom8010013 issn: 2218-273X Biomolecules 8 (2018) http://hdl.handle.net/10261/180756 openAccess Gad m 1 calcite calcium carbonate precipitation EF-hand motif amyloids Artículo 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 Article in Journal/Newspaper atlantic cod Digital.CSIC (Spanish National Research Council) Biomolecules 8 1 13 |
institution |
Open Polar |
collection |
Digital.CSIC (Spanish National Research Council) |
op_collection_id |
ftcsic |
language |
English |
topic |
Gad m 1 calcite calcium carbonate precipitation EF-hand motif amyloids |
spellingShingle |
Gad m 1 calcite calcium carbonate precipitation EF-hand motif amyloids Castellanos, M. Torres-Pardo, A. Rodríguez-Pérez, R. Gasset, M. Amyloid assembly endows gad m 1 with biomineralization properties |
topic_facet |
Gad m 1 calcite calcium carbonate precipitation EF-hand motif amyloids |
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 |
format |
Article in Journal/Newspaper |
author |
Castellanos, M. Torres-Pardo, A. Rodríguez-Pérez, R. Gasset, M. |
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/10261/180756 https://doi.org/10.3390/biom8010013 |
genre |
atlantic cod |
genre_facet |
atlantic cod |
op_relation |
MINECO/ICTI2013-2016/BFU2015-72271-EXP Publisher's version Sí doi:10.3390/biom8010013 issn: 2218-273X Biomolecules 8 (2018) http://hdl.handle.net/10261/180756 |
op_rights |
openAccess |
op_doi |
https://doi.org/10.3390/biom8010013 |
container_title |
Biomolecules |
container_volume |
8 |
container_issue |
1 |
container_start_page |
13 |
_version_ |
1766357920017022976 |