Targetting difficult-to-reach areas affected by disease could become a lot easier as researchers have developed a new system to make nanobodies, the efficient tiny cousins of antibodies, the defensive proteins deployed by the immune system, more accessible.
Nanobodies could be much more efficient than antibodies in attacking diseased cells, but scientist have so far lacked an efficient way of identifying the nanobodies, which are more closely tuned to their targets.
"Nanobodies have tremendous potential as versatile and accessible alternatives to conventional antibodies, but unfortunately current techniques present a bottleneck to meeting the demand for them," said study author Michael Rout from the Rockefeller University in the US.
"We hope that our system will make high-affinity nanobodies more available, and open up many new possible uses for them," Rout added.
The study was conducted using llamas. They were injected with foreign proteins.
"The key was to figure out a relatively fast way of determining the genetic sequences of the antibodies that bind to the targets with the greatest affinity. Up until now obtaining these high-affinity sequences has been something of a holy grail," said Brian Chait, professor at the Rockefeller University.
"Once those sequences are obtained, it is easy to engineer bacteria to mass produce the antibodies," Chait added.
The researchers determined partial sequences of the amino acids that made up the protein of the nanobodies with a technique known as mass spectrometry.
Using a computer algorithm called 'llama magic', the researchers matched the composition of the highest affinity nanobody with the original genetic sequence.
The study appeared in the journal Nature Methods.
