Highly tunable biotemplating methods expand options for nanostructure synthesis
CamBio uses microtubules, which are protein structures inside cells. The silver nanoparticle chains synthesized along microtubules extending throughout the cell interior could be observed using electron microscopy, indicating that they can be used as SERS substrates. Credit: Advanced Science (2024). DOI: 10.1002/advs.202406492
The joint research team developed a highly tunable biotemplate method that utilizes specific internal proteins in biological samples. The study is published in the journal Advanced Science.
Existing biotemplating methods mainly utilize only the outer surface of biological samples or are limited in dimensions and sample size, which limits the ability to utilize structure-function relationships of various biological structures, making it difficult to develop functional nanostructures. is difficult to produce.
To solve this problem, the research team investigated ways to utilize various biological structures within cells while maintaining high malleability.
As a result of their research, the research team developed a labeled biostructure (abbreviated as CamBio) that can selectively synthesize nanostructures of various specificities and sizes from specific protein structures in biological samples composed of various proteins. We have developed a method for converting the material into an advanced material.
The CamBio method combines various manufacturing and biological techniques to ensure high retunability of functional nanostructures that can be produced from biological samples.
Functional nanostructures made with CamBio are used for surface-enhanced Raman spectroscopy (SERS) substrates used for substance detection by repeatedly attaching antibodies, arranging cells in a fixed shape, and slicing tissue into thin layers. Performance has been improved.
A method to ensure tunability at the cell level using CamBio. We provide an example of integrating iterative antibody labeling and cell patterning techniques with CamBio to control properties by integrating structural tunability with biotemplates. Credit: Advanced Science (2024). DOI: 10.1002/advs.202406492
The researchers found that the nanoparticle chains, created by exploiting intracellular protein structures through a process of repeated labeling with antibodies, can be easily controlled and improve SERS performance by up to 230%.
The research team included Professors Jae-Byum Chang and Yeon Sik Jung, and first author Ph.D. Candidate Son Dae-hyun, Dr. Son Chan-woo, KAIST’s Dr. Cho Seung-hee, and others.
Additionally, the researchers tapped into intracellular structures, using frozen sections to obtain samples of muscle tissue inside meat and running the CamBio process to create substrates with periodic bands of metal particles. I succeeded in doing so. This substrate fabrication method not only allows for large-scale fabrication using biological samples, but also shows that it is a cost-effective method.
CamBio, developed by the research team, is expected to expand the range of biological samples that can be prepared for a variety of uses, and is expected to be used as a means of solving problems faced in a variety of research fields.
How to use CamBio to ensure tunability at the tissue level. We demonstrate that by combining frozen tissue sectioning technology to utilize proteins within muscle tissue, we successfully fabricate a substrate with a periodic nanoparticle band pattern, enabling large-area sample acquisition and cost competitiveness. . Credit: Advanced Science (2024). DOI: 10.1002/advs.202406492
Lead author Dae-Hyeon Song said, “Through CamBio, we have comprehensively accumulated bioprototyping methods that can utilize a greater variety of protein structures.
“When combined with the latest biological technologies such as gene editing and 3D bioprinting, and new materials synthesis techniques, biological structures have the potential to be used in a variety of application fields.”
Further information: Dae-Hyeon Song et al., Highly Tunable, Nanomaterial-Functionalized Structural Temptting of Intracular Protein Structures Within Biological Species, Advanced Science (2024). DOI: 10.1002/advs.202406492
Provided by Korea Advanced Institute of Science and Technology (KAIST)
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