Dissipationeless waves for information transfer in neurobiology

Danko Georgiev & James Glazebrook, Kanazawa University & Eastern Illinois University

Informatica, 30 (2006) pp. 221-32

Solitons or solitary wave quanta can retain their form and velocity when undergoing collisions. Pairs of soliton waves are seen to pass through one another. The authors refer to the work of Davydov on solitons (1&2.), which is seen as a basis for proposing dissipationless energy transfer in organic matter, and in particular influences on dendritic and axonal microtubules, information processing within neurons and generation of synapses.

The cytoskeleton dynamically regulates neurons, and is formed by self-assembling protein networks. Microtubules are the main constituents of this network, and interact with other cytoskeletal structures such as actin filaments, microtubule associated proteins (MAPs), and various scaffold proteins. Microtubules are formed out of sub-units of tubulin protein. A study by (3. Sackett, 1995) revealed that each tubulin has a 4-5 nanometre ‘tail’ that is extremely sensitive to environmental conditions and local electrical fields, and as a result produces a large number of different conformations (4. Georgiev, 2003a). It is emphasised that microtubules are not passive tracts for molecules to be moved along, and relative to this, it has been shown that the tubulin tails can modulate the function of the motor protein, kinesin (5. Skiniotis et al, 2004). Tubulin tails can also attach to MAPs, protein kinases and phosphatises, while microtubule anchored enzymes such as phosphatases and kinases are tuned by microtubules. These processes may involve soliton assisted tunnelling (6. Sutcliffe & Scrutton, 2000).

The cytoskeleton constitutes a protein surface, to which water molecules attach, and this allows the water to become ordered. Ordered water molecules interact via hydrogen bonds. On the basis of another study (7. Jibu et al, 1997), it is suggested that the ordering of water on the microtubule surface creates long-wave correlations of electric dipoles or dipole wave quanta (DWQ). It is suggested that the water molecules and the tubulin tails react with the local electromagnetic field to allow solitons to travel along the microtubules. Coherence time is estimated at 10-15 picoseconds, to be compatible with the action of protein.

The authors further suggest the possibility that the complex of the presynaptic scaffold protein network links mictotubules to synaptic vesicles. This is suggested to involve the protein synaptotagmin, and would connect microtubules directly to the firing of synapses.

1.) Davydov, A. (1982) – Biology and Quantum Mechanics – Pergamon Press
2.) Davydov, A. (1991) – Solitons in Molecular Systems – Kluwer, Dordrecht
3.) Sackett, D. (1995) – Structure and function in the tubulin dimer and the acid carboxyl terminus – Subcellular Biochemistry Proteins, 24, pp. 255-302
4.) Georgiev, D. (2003a) – Electronic and magnetic fields inside neurons – cogprints.org/3190/
5.) Skiniotis, G. et al (2004) – Modulation of kinesin binding by the C-termini of tubulin – The EMBO Journal, 23, pp. 989-9
6.) Sutcliffe, M. & Scrutton, N. (2000) – Enzyme catalysis – Trends in biochemical science, 25, (2000), pp. 405-8
7.) Jibu, M. et al (1997) – Evanescent photon and cellular vision – Biosystems, 42, pp. 65-73

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