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Significant findings about protein architecture may aid in drug design, generation of nanomaterials
Date:4/9/2010

surprisingly, to stabilize the structure by removing other side chains.

Understanding the assembly of the nanocage could open the door to drug design that will disrupt the structure and function of defective proteins that cause or contribute to disease. It also may aid in the creation of biological nanostructures in which scientists can grow special particles and materials with a variety of properties and applications.

"Cell biology provides many structures that are on the nanoscale and have amazing complexity and symmetry," Orner said. "The problem is that many of these structures are, like ferritin, self-assembled proteins, and, if we are going to use them for nanomaterials applications, we need to understand the fundamentals that make them form this way naturally."

Orner and his team members are particularly interested in growing nanoparticles of precise dimensions inside ferritin shells. Already, they have developed a new method to grow gold nanoparticles in them.

"Slight deviations in size or shape can radically change nanoparticles' properties, particularly in the case of metals and semiconductors," Orner said. "Our ferritin proteins are hollow, so, when we grow mineral or metal clusters inside them, the growth stops when the nanoparticles reach the limits of the protein shell."

By studying the rules that control the folding and assembly of such a protein in nature, Orner said, the investigators hope to be able to manipulate them one day to create new proteins with novel sizes and shapes and, therefore, generate nanoparticles of novel sizes and shapes inside them.

"Those nanoparticles could be used for in-vitro assays to do high-throughput drug screening of some protein-protein interactions involved in virus infection and cancer, for example," he said.

Orner's team included doctoral students Yu Zhang and Rongli Fan, undergraduate students Siti Raudah, Huihian Teo and Gwenda Teo, and scholar X
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Contact: Angela Hopp
ahopp@asbmb.org
301-634-7389
American Society for Biochemistry and Molecular Biology
Source:Eurekalert  

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