Protein disorder-order interplay to guide the growth of hierarchical mineralized structures.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 29858566.
- Also identified by DOI 10.1038/s41467-018-04319-0 and PMC identifier 5984621.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
A major goal in materials science is to develop bioinspired functional materials based on the precise control of molecular building blocks across length scales. Here we report a protein-mediated mineralization process that takes advantage of disorder-order interplay using elastin-like recombinamers to program organic-inorganic interactions into hierarchically ordered mineralized structures. The materials comprise elongated apatite nanocrystals that are aligned and organized into microscopic prisms, which grow together into spherulite-like structures hundreds of micrometers in diameter that come together to fill macroscopic areas. The structures can be grown over large uneven surfaces and native tissues as acid-resistant membranes or coatings with tuneable hierarchy, stiffness, and hardness. Our study represents a potential strategy for complex materials design that may open opportunities for hard tissue repair and provide insights into the role of molecular disorder in human physiology and pathology.
Medical subject headings
- Calcification, Physiologic
- Dentin
- Elastin
- Intrinsically Disordered Proteins
- Minerals