Researchers in Singapore are reporting this week that they have gleaned key insights into the architecture of a protein that controls iron levels in almost all organisms. Their study culminated in one of the first successful attempts to take apart a complex biological nanostructure and isolate the rules that govern its natural formation.
The Nanyang Technological University team's work on the protein ferritin, the results of which appear in this week's issue of the Journal of Biological Chemistry, is expected to have significant ramifications on the fields of drug design and nanomaterials.
"Engineering the structure of a protein is one of the ultimate dreams of structural biologists," wrote one of the journal's peer reviewers, "and approaching that dream is greatly enabled through studies aimed at finding out what governs the nanoarchitecture of the protein."
Brendan P. Orner, the assistant professor who oversaw the team's work, described the protein ferritin as a potential model for explaining complicated protein structure in general.
Across the biological kingdoms, ferritin regulates the distribution of iron, which is necessary for a number of cellular functions but also forms reactive ions that can be lethal to cells. Shaped like a spherical nanocage, ferritin is made up of 24 proteins, and it sequesters the reactive iron ions in its hollow interior. In humans, ferritin prevents iron deficiency and overload.
"The rules that govern self-assembling nanosystems, like the ferritin model, are poorly understood," Orner explained. "We systematically analyzed the interactions between the 24 ferritin units that make up the nanocage and identified the hot spots that are crucial to the cage's formation."
Their goal was to discover which amino acids are responsible for assembling the cage, and they found that it is possible to both disassemble ferritin by removing single side chains of amino acids and,
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American Society for Biochemistry and Molecular Biology