GIULIANO PREPARATAS CONTRIBUTION TO THE ION CYCLOTRON RESONANCE EXPERIMENTS

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GIULIANO PREPARATAS CONTRIBUTION TO THE ION
CYCLOTRON RESONANCE EXPERIMENTS

• Mikhail Zhadin
• Institute of Cell Biophysics
• Pushchino, Moscow Region, Russia

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A bridge between QED and Medicine

• In one of his last works (Preparata, 2000.
  Rivista di Biologia/ Biology Forum 93 467-512),
  finishing the description of main ideas of his
  remarkable QED theory, Giuliano Preparata wrote
• I shall end this presentation by briefly
  describing what the new physics has been able to
  build of the first section of the bridge towards
  Medicine. This section will concentrate on three
  arches
• (i) the new physics of water (ii) a
  possible origin of coherence in cell tissues
  (iii) the interaction of very weak, low frequency
  magnetic fields with the ions systems of the
  cell.
• Analyzing point (iii), Preparata referenced
  the work by him and his pupils, which was
  published after his untimely death (Del Giudice,
  Fleischmann, Preparata, Talpo, 2002.
  Bioelectromagnetics, 23, 522-530).

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The situation in Bioelectromagnetics in 90-th

• In 1985 Liboff and Blackman et al. discovered
  unusual resonance effects of simultaneous weak
  (several tens of µT) DC and low frequency AC
  magnetic fields (MFs) in the form of a change in
  calcium ion concentration in the nervous tissue.
  These effects were only observed at the cyclotron
  frequency of calcium ions. Later, many works,
  which were performed in different organizations
  and on different biological objects, confirmed
  the real existence of such sort of effects.
  However, the physical mechanisms of these effects
  in the rather dense liquid medium remained
  unclear. The question, what kind of ions free
  or bound ones are the main target for MFs
  action, was not solved either. The unusual
  narrowness of resonance peaks in MFs effects
  evidently pointed to the extremely low level of
  damping and viscosity within microvolumes in
  biological aqueous solutions.

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Resonance peak (Liboff et al. 1987. In
Mechanistic approaches to interaction of
electric and electromagnetic fields with living
systems". N Y 109)Half-width is about 5 Hz
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Our experiments with amino acid solutions

• In the beginning of 90-th (in Laboratory of
  Prof. Zhadin, Institute of Cell Biophysics,
  Russia) we performed a series of experiments for
  investigation of action of weak low frequency AC
  MF combined with parallel DC MF on an aqueous
  solution of an amino acid. The main attention was
  paid to the glutamic acid solution, because it
  gave the most prominent effects as compared with
  other amino acids. Choosing this simplest system
  for investigation, we hoped to understand whether
  MFs are able to influence on the ensemble
  consisting of free particles alone and to
  estimate the minimal threshold of the AC MF for
  inducing an effect. The value of DC MF was chosen
  to be close to the geomagnetic one (about 40 µT).
  In the experiments we measured the value of an
  electric current passing through the solution.

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Experimental installation

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Results and their publication

• For each tested value of the AC MF amplitude
  we scanned the AC MF frequency around the
  cyclotron frequency corresponding to amino acid
  ion. To our great surprise, we revealed the
  prominent effect already at the AC MF amplitude
  measured with several tens of nT in the form of
  narrow (less than one Hz in half-width) resonance
  peak (shown in the next slide). In 1994 we
  submitted the manuscript with our results to
  Bioelectromagnetics journal. But its publication
  was delayed till the time when Zhadin would give
  the physical explanation of a possible mechanism
  of this phenomena. The manuscript was published
  (Zhadin et al., 1998. Bioelectromagnetics, 19,
  41-45 ) four years later, after Zhadin submitted
  another manuscript with a theory of action of
  combined MFs on thermal motion of an ion within a
  macromolecule or microcrystal (Zhadin, 1998.
  Bioelectromagnetics, 19, 279-292) elaborated by
  him. These results were replicated by Del
  Giudice et al. (2002) and Comisso et al. (2006)
  in Italy, and Pazur (2004) in Germany.

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Resonance peak in the current through the
solution

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Preparatas theory of MFs influence on
conductivity in aqueous solution

• G. Preparata and his coworkers not only paid
  their attention to the above experiments with
  aqueous amino acid solutions, giving them a high
  estimate and successfully replicating them, but
  also elaborated a physical theory of these
  effects on the base of Preparatas QED theory of
  condensed matter. In their brilliant work (Del
  Giudice et al., 2002) they studied the motion of
  amino acid ions in coherence domains (CDs where
  the coherent water has essentially reduced
  viscosity. They showed that under the influence
  of DC MF the ions rotate along CDs borders
  without loss of their kinetic energy, constantly
  suffering internal reflectance, and that AC MF
  with the cyclotron frequency corresponding to
  charge-to-mass ration of the given ions leads to
  the gradual increase in the energy of these ions
  and to their escape from the CDs to the
  incoherent surrounding medium. These processes
  cause the short-term increase of the current
  through the exposed solution. Thus all main
  objections of critics of this line in
  Bioelectromagnetics were overruled.

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Development of Preparatas ideas

• The fruitful theory by Preparata and his
  coworkers provided further development of
  understanding of forming of resonance phenomena
  in aqueous solution of amino acids. Preparata
  promoted formation of mutual connections between
  Italian and Russian scientists that led to their
  successful collaboration. Leaning upon the above
  elaboration by Preparata and his coworkers we
  were able to understand some problems in more
  details 1) How and in what forms do the amino
  acid ions enter inside coherence domains (CDs)?
  2) How do they participate in formation of
  coherent oscillations of molecules within CDs,
  and 3) What is the mechanism of successive cyclic
  change in different ionic forms in the solution
  under the influence of MFs? These problems were
  considered in our recent work (Zhadin and
  Giuliani. 2006. Electromagnetic Biology and
  Medicine, 25 227-243).

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Mixed CDs in aqueous amino acid solution

• Amino acid ions can have different ionic
  shapes depending on pH of the aqueous solution.
  At pH3, as in our experiments, glutamic acid
  ions have a zwitterionic form, that is dipole
  with a rather long distance between its two
  charges and with a comparatively big dipole
  moment. After preparing the solution, zwitterions
  take places in the solution by big clusters and,
  at the forming of CDs, are inevitably captured by
  them. Owing to the carboxylic group, a zwitterion
  spectrum has transition close to basic coherent
  frequency 12.06 eV of water molecules and its
  molecule easily transform into the usual ionic
  form, because this frequency is close to the
  ionization potential of a glutamic acid molecule.
  Thanks to low viscosity inside CDs, MFs increase
  kinetic energy of of these ions and withdraw them
  out of CDs by means of the mechanism considered
  by Preparata and his coworkers. When escaping
  CDs, the glutamic acid ions come back into the
  surrounding incoherent medium with pH3 and
  acquire the zwitterionic form again.

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What molecules are able to participate in mixed
CDs forming?

• Far from each type of molecules are able to
  participate in mixed CDs forming. The specific
  spectral properties and special ion forms are
  necessary for this. The molecules which are
  capable of participation in CDs forming can be
  not only in single form, but in the form of
  molecules bound in a complicated macromolecule
  like amino acids within a protein molecule. In
  the first case, CDs include these molecules, and
  in the second case, when the macromolecule is
  bigger than CDs, the CD sits on them. One mixed
  CD can bind two macromolecules or two parts of
  the same macromolecule, including two particular
  amino acids at two parts of the same protein
  molecule. High stability of CDs evidences high
  binding energy of molecules within them which is
  much more than energy of thermal noises and of
  hydrogen bonds. Such CDs can provide strong bonds
  between macromolecules or different parts of the
  same macromolecule (tertiary or quarternary
  structures).

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Thank you for your attention, my dear
friends !