ISIS Report 14/01/05
Mobile Phone Turns Enzyme Solution into A Gel
A highly reproducible non-thermal effect of mobile phones depends on
interaction between protein and water. Dr.
Mae-Wan Ho says it brings us closing to understanding the biophysics
involved in how weak electromagnetic radiation can have biological
effects.
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Serious brain damage unaccounted for
The most striking effect of exposure to the radio-frequency (RF)
radiation from mobile phones is damage to the brain and brain cells of rats
(see "Mobile phones & brain damage"
SiS24), which
were found at levels of exposure far below the current safety limits. After
just two hours of such exposure, blood albumin leaked into the brain causing
brain cells to die; and the effects lasted for at least 50 days after a single
exposure. But no clear mechanism has emerged to explain this or other
‘non-thermal’ effects of electromagnetic fields (EMFs) even after a
concerted, Europe-wide research programme (see "Confirmed: mobile phones break DNA
and scramble genomes", this series).
I have suggested that phase changes in cell water triggered by EMFs may
be involved in causing many biological effects, but there has been a complete
lack of support for research in that area (see "Electromagnetic fields,
leukaemia and DNA damage", SiS24).
Now, new research findings make that suggestion a great deal more
plausible.
A ‘breakthrough’ in identifying mechanisms?
Researchers at the University of Rome in Italy led by Mario Barteri in
the Chemistry Department report striking changes in a solution of an enzyme
after exposure to RF radiation from mobile phones. This is the first time such
a simple, reproducible, in vitro system has been devised to study the
effects of EMFs.
The enzyme, acetylcholine esterase, involved in transmitting nerve
signals from the brain to the skeletal muscle, has been purified and studied in
great detail and commercial preparations are readily available. The researchers
chose to study the acetylcholine esterase from the electric eel.
The enzyme was dissolved in a buffer solution in water and identical
samples were exposed to RF radiations within the range of 915-1822 megahertz
for 1 to 50 minutes, while the control (unexposed) was wrapped securely in
aluminium foil to screen the RF radiations. A commercial cellular phone was
used as the source of RF radiation at a specific absorption rate (SAR) of
0.51W/kg, with the mobile phone operating in the receiving mode.
After exposing the enzyme solution, the researchers used a range of
physical measurement techniques to characterise the changes.
First they passed the solutions down a gel filtration column, which
separates protein molecules by size. At short irradiation times between 1 to 10
min, no difference from the unexposed control was found; a single protein peak
was identified, representing the enzyme in its usual ‘dimeric’ form
consisting of two protein units associated together. However, after 20 min or
more, a new peak was formed in addition to the old; the new peak representing
the monomeric or dissociated form of the protein. This profile remained stable
after one day at room temperature, showing that irreversible change had taken
place in the solution.
Measurements on the rate constants of the enzyme activity similarly
indicated that up to 10 min of RF radiation exposure had no effect, but after
20 min or more, the rate constants changed dramatically, which was consistent
with previous findings from another laboratory reporting increase in the enzyme
activity in mice after twenty minutes exposure to mobile phone radiation.
This change in the kinetic properties of the enzyme was apparently not
accompanied by change in the three-dimensional shape (conformation) of the
protein, at least as measured by circular dichroism (a technique for
characterising the shape of molecules based on measuring the unequal absorption
of right and left plane-polarized light).
Measurement by X-ray scattering, however, revealed a drastic change in
the collective organisation of the protein in solution, which suggested that a
phase of ‘hydrogel’ had separated out from the main solution. This
hydrogel was made up of monomeric protein molecules associated with lots of
water molecules to form a collective phase.
Finally, the researchers took a scanning electron micrograph of the
control and the exposed sample, which showed up the marked difference. The
native, unexposed sample appeared as a random suspension of enzyme molecules;
whereas the irradiated sample appeared as a highly oriented sample with a
regular periodic pattern.
RF radiation trigger interaction of enzyme protein with water
The enzyme protein has a very strong negative charge near the entrance
to the ‘gorge’ containing the active site (where the substrate is
bound), which gives a strong dipole (separated positive and negative electric
charges) oriented along gorge. This makes the protein sensitive to fluctuations
of the electric field generated by the RF radiation from the cellular phone;
which in turn perturbs the dipoles of the water molecules, resulting in the
formation of the hydrogel.
As a further check, the researchers carried out nuclear magnetic
resonance (NMR) measurements on the proton spin relaxation times
(T1) of
the water molecules. For bulk water, the relaxation time was 2983+27;
for native enzyme dissolved in water, it was 470+25; for
enzyme exposed to RF radiation for 20 min, it was 260+32, and exposed
for 50 min, 220+38. The results, once again, are
consistent with the increased interaction of enzyme protein with water
molecules that one would find in a hydrogel.
The researchers said, rightly, that the results "cannot be used to
conclude whether exposure to RF during the use of cellular phone can lead to
any hazardous health effect"; but "they may be a significant model to verify
these effects on other biological systems."
I believe however that these results are important in contributing to
our understanding of ‘non-thermal’ effects: they are mediated through
the collective structure of water, especially as conceived by a number of key
researchers in biological water.
Collective structure of water important
The phenomena observed by Barteri and co-workers depend on the
collective structure of water, which effectively sums and amplifies the effect
of weak EMFs. It provides the mechanism for non-thermal effects that
conventional scientists find so "inconceivable", largely out of ignorance.
The results also appear to be consistent with the work of researchers
who made pioneering discoveries on water in the cell. Gilbert Ling, in
particular, first proposed that water molecules form polarised multi-layers
over extended protein surfaces inside the cells (see "Strong medicine for cell
biology" SiS
24). This proposal received remarkable confirmation recently in an in
vitro system (see "Water forms massive exclusion zones",
SiS23) and in
the cell (see "What’s the cell really like?"
SiS24); and is
also consistent with findings in my own laboratory that the water in living
organisms is an intrinsic part of the liquid crystalline continuum of the body
(see The Rainbow and the Worm,
the Physics of Organisms).
The hydrogel created by Barteri and colleagues after exposing the enzyme
solution to RF radiation are very likely to consist of multilayers of polarised
water molecules on extended protein surfaces. The RF radiation acts as a
trigger to dissociate the protein dimers into monomers and to interact with
water; without however, destroying enzyme activity; if anything it appeared to
have increased enzyme activity.
The findings of Barteri’s team are also consistent with the
proposals of Martin Chaplin and Frank Mayer, that water switches between a
low-density and a high-density phase with very different interactions between
proteins and water molecules that change enzyme activities and cell function
(see "the importance of cell water" and "What’s the bacterium really
like?", SiS24).
Martin Chaplin expresses surprise at the result, as did the authors of
the research paper. "The jellification would seem to be very specific to the
properties of that particular enzyme. The process by which the radiation
increases the hydration of the protein and causes its dissociation can be
explained, but [is possibly] an extreme case of what can occur." He adds, "The
work does show how the power of water to hydrate molecules increases when the
‘normal’ hydrogen bonding is disrupted; and also that the change in
hydration may not be readily reversible. I doubt if any present computer model
of water could reproduce this phenomenon."
We can no longer accept the mantra that there is no "conceivable"
mechanism that could explain non-thermal effects of EMFs, and that the current
EMF exposure limits may well be harmful.
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