Press releases
Please quote Nature Materials as the source of these items.
October 2002
Mutant molecular motors
It may be the stuff of nanotechnology dreams (or nightmares?) but the idea of building tiny molecular machines came one step closer this month with the 'switching on' of a biomolecular motor by Carlo Montemagno and colleagues. As they report in the November issue of Nature Materials, Montemagno's team has designed and built a simple motor-powered device by genetically modifying a well-known biological protein, the enzyme F1-ATP synthase.
By spinning continuously inside cells, the protein ATP synthase generates ATP - the fuel that powers most cellular activity. The F1 fragment of ATP synthase functions as a rotary motor and two years ago Montemagno and co-workers modified its activity by attaching nanoscale propellers to the enzyme. This time the researchers have created a mutant F1 fragment containing a zinc-binding site that functions as a chemical switch for controlling the motor activity.
When zinc is absent, the mutant motor can operate, but switches off when zinc is present. Such control is essential for building integrated nanodevices from single-molecule components. The authors hope to build future devices in which the chemical switch allows sensing and feedback control of the motor and related components.
