Science in Society Archive

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.

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.

Article first published 14/01/05


  1. Barteri M, Pala A and Rotella S. Structural and kinetic effects of mobile phone microwaves on acetylcholinesterase activity. Biophysical Chemistry 2005, 113, 245-53.
  2. Ling G. Life at the Cell and Below-Cell Level, The Hidden History of a Fundamental Revolution in Biology, Pacific Press, New York 2001.
  3. Mayer F. Cytoskeletons in prokaryotes – Status report and hypothesis. Cell Biol Internat 2003, 27, 429-38.
  4. Edelman L. Freeze-dried and resin-embedded biological material is well-suited for ultrastructure research. J Microscopy 2002, 207, 5-26.
  5. Zheng J-M, and Pollack GH. Long-range forces extending from polymer-gel surfaces. Physical Review E 2003, 68, 031408.

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