ArticleACS omega2016
Aragonite-Associated Mollusk Shell Protein Aggregates To Form Mesoscale "Smart" Hydrogels.
Article in ACS omega, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Research progress on formation mechanism of pearl.Heliyon · 2024Article
- Stimuli-Responsive Protein Hydrogels: Their Design, Properties, and Biomedical Applications.Polymers · 2023Review
- Application of fungal copper carbonate nanoparticles as environmental catalysts: organic dye degradation and chromate removal.Microbiology (Reading, England) · 2021Article
- Composite Materials Design: Biomineralization Proteins and the Guided Assembly and Organization of Biomineral Nanoparticles.Materials (Basel, Switzerland) · 2019Review
- Sea Urchin Spicule Matrix Proteins Form Mesoscale "Smart" Hydrogels That Exhibit Selective Ion Interactions.ACS omega · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the mollusk shell there exists a framework silk fibroin-polysaccharide hydrogel coating around nacre aragonite tablets, and this coating facilitates the synthesis and organization of mineral nanoparticles into mesocrystals. In this report, we identify that a protein component of this coating, n16.3, is a hydrogelator. Due to the presence of intrinsic disorder, aggregation-prone regions, and nearly equal balance of anionic and cationic side chains, this protein assembles to form porous mesoscale hydrogel particles in solution and on mica surfaces. These hydrogel particles change their dimensionality, organization, and internal structure in response to pH and ions, particularly Ca(II), which indicates that these behave as ion-responsive or "smart" hydrogels. Thus, in addition to silk fibroins, the gel phase of the mollusk shell nacre framework layer may actually consist of several framework hydrogelator proteins, such as n16.3, which can promote mineral nanoparticle organization and assembly during the nacre biomineralization process and also serve as a model system for designing ion-responsive, composite, and smart hydrogels.
Identifiers
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Registered trials
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