Nowadays, biomolecular
motor-based miniaturized lab-on-a-chip devices
have been attracting much attention for their wide range of nanotechnological
applications. Most of the applications are dependent on the motor-driven
active transportation of their associated filamentous proteins as
shuttles. Fluctuation in the movement of the shuttles is a major contributor
to the dispersion in motor-driven active transportation, which limits
the efficiency of the miniaturized devices. In this work, by employing
the biomolecular motor kinesin and its associated protein filament
microtubule as a model active transport system, we demonstrate that
the deep-sea osmolyte trimethylamine
N
-oxide (TMAO)
is useful in regulating the fluctuation in the motility of microtubule
shuttles. We show that the motional diffusion coefficient, a measure
of the fluctuation in the movement of the kinesin-propelled microtubules,
gradually decreases upon increasing the concentration of TMAO in the
transportation system. We have been able to reduce the motional diffusion
coefficient of microtubules more than 200 times by employing TMAO
at a concentration of 2 M. We also show that upon elimination of TMAO,
the motional diffusion coefficient of microtubules can be restored,
which confirms that TMAO can be used as a tool to reversibly regulate
the fluctuation in the sliding movement of kinesin-propelled microtubule
shuttles. Such reversible regulation of the dynamic behavior of the
shuttles does not require sacrificing the concentration of fuel used
for transportation. Our results confirm the ability to manipulate
the nanoscale motion of biomolecular motor-driven active transporters
in an artificial environment. This work is expected to further enhance
the tunability of biomolecular motor functions, which, in turn, will
foster their nanotechnological applications based on active transportation.