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Professor Sadler with diagram of iron banded fibril.
Photo �: University of Warwick
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Transferrin takes up iron out of bloodstream
and transports it by a method that combines it with carbonate to bind
to two sites on the surface of the transferrin protein. It then curls
around the iron and seals it in, almost like a Venus flytrap plant, to
prevent it from interacting with anything else until it reaches where
it is needed and can safely be used.
The research team led by Professor Peter Sadler from the University of
Warwick, and Professor Sandeep Verma from the Indian Institute of
Technology, found that if they took transferrin and left it to dry out
on a surface, molecules of the safe transporter of iron assembled
themselves into tendril - or worm-like fibrils. Even more
interestingly the iron that was once safely wrapped up inside the
transferrin now appeared to be settling along the length of these
fibrils plating them in a series of spots or bands along the length of
the tendril shape. This leaves the iron dangerously exposed and
available to interact in ways that could cause cell damage.
Deposits of iron exposed in this way and found in the brain are a
possible cause of some forms of Parkinson�s, Alzheimer�s and
Huntington�s diseases. Until now there has been no real idea as to how
iron becomes deposited there in such a dangerous way. As it is
essential for the brain to have iron safely delivered to it, this
observation could provide the first real clue as to how that iron
comes to be deposited there in such a dangerous way. The research
chemists who led this study hope that neurology researchers will be
able to build on this work to gain more understanding of how these
forms of Parkinson�s, Huntington�s and Alzheimer�s occur and how they
can be countered.
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