eesti teaduste
akadeemia kirjastus
Estonian Journal of Engineering

Use of infrared and visible light radiation as modulator of protein activity; pp. 107–123

Full article in PDF format | doi: 10.3176/eng.2008.2.02

Elena Pirogova, Irena Cosic, John Fang, Vuk Vojisavljevic

In this study we discuss the possibility of modulating protein activity using infrared and visible light radiation based on the concepts of protein activation incorporated in the resonant recognition model (RRM). Application of the RRM approach includes prediction of the functional “key” amino acids in the protein molecule, prediction of the protein active site, design of de-novo peptides with the desired function and determination of the specific electromagnetic radiation frequency that may activate protein sequence. The theoretical basis behind the RRM model expounds a potential interaction mechanism between electromagnetic radiation and proteins as well as protein–protein interactions. Here the RRM hypothesis of protein activation is experimentally validated via irradiation of the L-lactate dehydrogenase enzyme by the electromagnetic field exposures in the range of 1140–1200 nm. In this paper we also present an application of the RRM to bioactive peptide design, and explore theoretically if proteins or DNA molecules can be activated by much lower frequencies, particularly in the microwave range (from 109 to 1010 Hz).

  1. Cosic, I. The Resonant Recognition Model of Macromolecular Bioactivity: Theory and Applica­tions. Birkhauser Verlag, Basel, 1997.

  2. Karu, T. Primary and secondary mechanisms of actions of visible to near-IR radiation on cells. Photochem. Photobiol., 1999, 49, 1–17.

  3. Kujawa, J., Zavodnik, L., and Zavodnik, I. Low-intensity near-infrared laser radiation-induced changes of acetylcholinesterase activity of human erythrocytes. J. Clinical Laser Med. Surgery, 2003, 21, 351–355.

  4. Adey, W. R. Biological effects of EMF. J. Cell Biochem., 1993, 51, 410–416.

  5. Blank, M. and Soo, L. Optimal frequencies for magnetic acceleration of cytochrome oxidase and NaK-ATPase reactions. Bioelectrochem. Bioenergetics, 2001, 53, 171–174.

  6. Fedoseyeva, G. E., Karu, T. I., Lyapunova, T. S., Pomoshnikova, N. A. and Meissel, M. N. The activation of yeast metabolism with He-Ne laser radiations-II. Activity of enzymes of oxidative and phosphorous metabolism. Lasers Life Sci., 1988, 2, 147–154.

  7. Blum, H. Carcinogenesis by Ultraviolet Light. Princeton University Press, Princeton, N.J., 1959.

  8. Nussbaum, E. L., Lilge, L. and Mazzulli, T. Effects of 630-, 660-, 810-, and 905-nm laser irradiation delivering radiant exposure of 1–50 J/cm2 on three species of bacteria in vitro. J. Clinical Laser Med. Surgery, 2002, 20, 325–333.

  9. Vojisavljevic, V., Pirogova, E. and Cosic, I. The effect of electromagnetic radiation (550 nm–850 nm) on l-Lactate Dehydrogenase Kinetics. Int. J. Radiation Biol., 2007, 83, 221–230.

10. Pirogova, E., Fang, Q., Akay, M. and Cosic, I. Investigation of the structure and function relationships of oncogene proteins. Proc. IEEE, 2002, 90, 1859–1868.

11. De Trad, C. H., Fang, Q. and Cosic, I. Protein sequences comparison based on the wavelet transform approach. Protein Eng., 2002, 15, 193–203.

12. Ciblis, P. and Cosic, I. The possibility of soliton/exciton transfer in proteins. J. Theor. Biol., 1997, 184, 331–338.

13. Biscar, G. Photon enzyme activation. Bull. Math. Biol., 1976, 38, 29–38.

14. Veljkovic, V. and Slavic, M. General model of pseudopotentials. Phys. Rev. Lett., 1972, 29, 105–108.

15. Veljkovic, V. A Theoretical Approach to Preselection of Cancerogens and Chemical Cancero­genesis. Gordon and Breach, New York, 1980.

16. Cosic, I. and Pirogova, E. Bioactive peptide design using the resonant recognition model. Nonlin. Biomed. Phys., 2007, 1(7), doi: 10.1186/1753-4631-1-7.

17. Fulton, A. B. and Isaacs, W. B. Titin, a huge, elastic sarcomeric protein with a probable role in morphogenesis. Bioessays, 1991, 13, 157–161.

Back to Issue