A Basic Matrix Protein Songin Selectively Promotes Aragonite Aggregation and Modulates Calcium Carbonate Crystallization in Hyriopsis cumingii
- 1Shanghai Ocean University , , ,
- 2Yangtze Delta Region Institute of Tsinghua University , , , ,
- 3University of Algarve , , Campus de Gambelas , ,
Abstract
In China, the pearl industry of Hyriopsis cumingii contributes approximately 80% of pearl production. Matrix proteins play crucial roles in shell and pearl biomineralization. However, the functions of basic matrix proteins in H. cumingii remain poorly understood. In this study, we identified a novel predicted secreted basic matrix protein, designated Songin, from the freshwater pearl mussel H. cumingii. Functional assays were performed using a chemically synthesized 53-amino-acid peptide corresponding to the predicted mature region of Songin. Songin transcripts showed a relative mantle-enriched expression pattern and were detected in dorsal mantle epithelial cells, suggesting a potential association with shell biomineralization. In the end point crystallization assay, Songin was associated with pronounced aggregation of mineral particles under Mg2+-containing aragonite-favoring conditions while exerting only minor effects on particle morphology in the calcite-favoring system. Raman spectroscopy supported the predominant polymorph assignments in the calcite-favoring and Mg2+-containing aragonite-favoring systems, and no obvious Songin-associated change in the predominant polymorph was detected under the tested conditions. Laser scanning confocal microscopy showed heterogeneous Cy5-associated fluorescence near localized regions of some mineral particles. Because free Cy5 and Cy5-labeled BSA controls were not included, nonspecific dye adsorption cannot be excluded, and these observations are regarded as preliminary qualitative information rather than evidence of specific crystal-surface binding. This study indicates that the synthetic mature-region Songin peptide was associated with pronounced mineral-particle aggregation under Mg2+-containing aragonite-favoring conditions in vitro, suggesting a potential role in mineral-particle assembly during shell biomineralization. These findings provide preliminary insight into the possible involvement of Songin in shell biomineralization.
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BibTeX
@article{fan2026basic,
title = {{A Basic Matrix Protein Songin Selectively Promotes Aragonite Aggregation and Modulates Calcium Carbonate Crystallization in Hyriopsis cumingii}},
author = {Leyu Fan and Jiali Liu and Maoxiao Peng and Xiaojun Liu},
journal = {ACS Omega},
year = {2026},
month = oct,
doi = {10.1021/acsomega.6c03325},
url = {https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c03325/5460467/A-Basic-Matrix-Protein-Songin-Selectively-Promotes},
note = {CC BY-NC-ND 4.0},
}
RIS
TY - JOUR
TI - A Basic Matrix Protein Songin Selectively Promotes Aragonite Aggregation and Modulates Calcium Carbonate Crystallization in Hyriopsis cumingii
AU - Leyu Fan
AU - Jiali Liu
AU - Maoxiao Peng
AU - Xiaojun Liu
PY - 2026
DA - 2026/10/28
JO - ACS Omega
DO - 10.1021/acsomega.6c03325
UR - https://pubs.acs.org/acsodf/article/doi/10.1021/acsomega.6c03325/5460467/A-Basic-Matrix-Protein-Songin-Selectively-Promotes
AB - In China, the pearl industry of Hyriopsis cumingii contributes approximately 80% of pearl production. Matrix proteins play crucial roles in shell and pearl biomineralization. However, the functions of basic matrix proteins in H. cumingii remain poorly understood. In this study, we identified a novel predicted secreted basic matrix protein, designated Songin, from the freshwater pearl mussel H. cumingii. Functional assays were performed using a chemically synthesized 53-amino-acid peptide corresponding to the predicted mature region of Songin. Songin transcripts showed a relative mantle-enriched expression pattern and were detected in dorsal mantle epithelial cells, suggesting a potential association with shell biomineralization. In the end point crystallization assay, Songin was associated with pronounced aggregation of mineral particles under Mg2+-containing aragonite-favoring conditions while exerting only minor effects on particle morphology in the calcite-favoring system. Raman spectroscopy supported the predominant polymorph assignments in the calcite-favoring and Mg2+-containing aragonite-favoring systems, and no obvious Songin-associated change in the predominant polymorph was detected under the tested conditions. Laser scanning confocal microscopy showed heterogeneous Cy5-associated fluorescence near localized regions of some mineral particles. Because free Cy5 and Cy5-labeled BSA controls were not included, nonspecific dye adsorption cannot be excluded, and these observations are regarded as preliminary qualitative information rather than evidence of specific crystal-surface binding. This study indicates that the synthetic mature-region Songin peptide was associated with pronounced mineral-particle aggregation under Mg2+-containing aragonite-favoring conditions in vitro, suggesting a potential role in mineral-particle assembly during shell biomineralization. These findings provide preliminary insight into the possible involvement of Songin in shell biomineralization.
SN - 2470-1343
ER -