Synthetic nanoparticles achieve complexity level of proteins

Researchers at Carnegie Mellon University showed that nanoparticles can achieve similar complexity to that of protein molecules. This potentially opens the window to the production of more robust medical drugs, computer processor chips, and materials. Rongchao Jin, a chemistry professor, conducted the study in his lab where the complex nanoparticle structures were made. Nanoparticles are one to one hundred nanometers in size and can be manually ordered to create molecule-sized structures such as incredibly thin tubes. In nanotechnology, a nanoparticle is defined as a group of particles that behaves as a unit in terms of its transport and properties. Researchers noticed self-forming patterns in some nanoparticles made from Au-133 and Au-246 — gold isotopes. The experimentation thus aimed to discover the cause of these specific patterns, especially those that resemble natural patterns.

The study revealed that the nanoparticles bond by maximizing interactions between atoms. The particles then match to others with symmetric crystal surface patterns. This process repeats until a high-complexity structure is formed — one that resembles the complexity of protein molecules.
Nanoparticles have several uses. They can be used for drug and gene delivery systems, tissue engineering, detection of proteins, probing of DNA structure, and the creation of fluorescent biological labels in disease research. One use of nanoparticles that excited researchers most is in targeted treatment of diseases. By ordering a specific matrix of nanoparticle structure, drug manufacturers could create drugs that are less destructive to healthy tissue and reduce side effects, yet attack toxic cells and viruses more effectively.

The study was funded by the Air Force Office of Scientific Research and the Camille Dreyfus Teacher- Scholar Awards Program. Other authors of the study include Carnegie Mellon graduate student Yuxiang Chen, University of Toledo’s Kristin Kirschbaum, and Kelly J. Lambright.