Chemists are fascinated by the cell’s ability to compartmentalize, and they have been trying to mimic it for years. Separate things like the nucleus, mitochondria, and other compartments keep otherwise incompatible biochemical processes functioning cohesively in one cell. One of the simplest compartments is a protein shell, like the capsid of a virus. Protein shells are usually highly organized structures with defined geometric shapes and sizes. Scientists have altered natural protein shells for a variety of purposes, from crystallizing inorganic nanoparticles to the delivery of drugs. In a new paper, they've engineered a capsule that can neutralize a toxic protein.
Bigna W�rsd�rfer, Kenneth Woycechowsky, and Donald Hilvert used directed evolution, where they specifically select for certain traits in a protein, to engineer a container that is able to control the catalytic activity of an enzyme called a protease from the HIV genome. Their capsule was made from a protein called lumazine synthase, found in the bacteria Aquifex aeolicus (AaLS). AaLS is an enzyme that is involved in the biosynthesis of riboflavin (vitamin B2); it normally forms icosahedral-shaped capsids made from either 60 or 180 identical subunits.
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