It have been unknown to many why our eyes, the most fragile system of our body are so resistant to bacterial infection. Tears are shed daily in our everyday life but beside lubricating our eyes, it has a eve more important function.
Bacteriologist Alexander Fleming discovered in human tears a germ-fighting enzyme which he named lysozome in 1922. He collected his own tears, then demonstrated its extraordinary power to exterminate bacteria infront of contemporaries at Britain’s Royal Society.
How is this possible? According to Philip Collins, a physics professor at University of California, Irvine, each molecule is essentially a set of rapacious jaws that latches onto microbial invaders, starts chomping and does not let go.
This motion allows enzyme to open huge holes in the bacteria, which cause the bacteria to explode.
Each tear you shed contains an armada of these enzymes, ready to gobble up germs before they infect the sensitive tissue around your eye. However to study these enzymes, the researchers must keep one of the molecules still. To do this they relied on a tiny technology: carbon nanotubes.
A lysozyme molecule was tethered by an amino acid to a nanotube. Then passed an electric current along the tube, turning the molecules into little transistor. When lysozyme sprang into action each bite of its jaws produce an electrical activity.
This signal was like “a microphone that allows us to listen in on the enzyme’s activity,” according to Collins.
This newly found technique was also used to study many other molecules. For further understanding on the processes used :

Resources:
- Choi, Y., Moody, I.S., Sims, P.C., Hunt, S.R., Corso, B.L., Perez, I., Weiss, G.A., and Collins, P.G. 2012. Single-Molecule Lysozyme Dynamics Monitored by an Electronic Circuit [online]. Science, 335 (6066): 319-324.
- Lysozyme Nanocircuits at UC Irvine. Youtube video. Accessed January 23, 2012.