Subject(s)
Cell Proliferation , Culture Media , Melanoma/pathology , Spectrophotometry, Infrared , Humans , Temperature , Tumor Cells, CulturedABSTRACT
The infrared spectroscopy method was used for investigation of hydrosol water spectral (frequency) characteristics in normal and malignant cells and tissues. Thus our earlies disclosure of an important and statistically significant difference in spectral (frequency) parameters of normal and tumor tissues was confirmed. The investigation explored in controlled hyperweak field effect on behavior of malignant cells and tissues. Significant results were obtained by treating cells and tissues with original holograms which induced normal cell/tissue frequency accord. As a result, tumor cell population growth both in cell culture and retransplanted neoplasms was inhibition.
Subject(s)
Breast Neoplasms/metabolism , Cell Proliferation/radiation effects , Infrared Rays , Breast Neoplasms/pathology , Humans , Spectrophotometry, Infrared , Tumor Cells, CulturedABSTRACT
Our data on spectral characteristics of water in blood plasma hydrosols from breast cancer patients and healthy subjects are presented. A substantial difference between the two groups was found. As it was shown by us earlier, in breast cancer patients, as well as in other cancer patients, changes in spectral characteristics of water influence tissue hydrosols of the whole body. They persist even after tumor is radically removed. Such differences were probably linked to those in water molecular resonance frequencies. Using infrared spectroscopy, we confirmed the evidence available on carcinogenic (promoting) effect of both native and synthetic estrogens. It is suggested that healthy adult women have a certain "frequency immunity" which protects from the monthly autogenous promoting influences of estrogens. Our findings may contribute to devising further therapeutic frequency-assisted means of impacting on malignant tissue hydrosols.
Subject(s)
Body Water/metabolism , Breast Neoplasms/blood , Plasma/metabolism , Female , Humans , Spectrophotometry, InfraredABSTRACT
Possible involvement of aqueous medium in distant signal transmission to target cells through solitons without formation of the ligand-receptor complexes is discussed. Temperature dependence of IR spectra for dipeptide and amino acid solutions in the far and near IR regions are presented, which prove principal possibility of such processes.
Subject(s)
Peptides/chemistry , Binding Sites , Biophysical Phenomena , Biophysics , Ligands , Models, Chemical , Protein Structure, Tertiary , Spectrophotometry, Infrared , Temperature , Water/chemistryABSTRACT
The effect of amino acids and low-molecular-weight peptides on the dynamics of water was studied. Water medium together with molecules of dipeptides and amino acids dissolved in it is considered as a complex of interacting anharmonic oscillators. It was shown that the temperature behaviour of this system is determined by nonlinear resonances, which give rise to both the phenomenon of self-synchronization in the whole system or its part and to the phenomena of phase instability and coherence decay, depending on the store of oscillatory energy. Dissolved molecules are also involved in these oscillations, and if the frequencies and amplitudes of their oscillations are within the range in which nonlinear resonance occurs, they can affect the movement of the whole system.
Subject(s)
Amino Acids/chemistry , Dipeptides/chemistry , Water/chemistry , Molecular Weight , TemperatureABSTRACT
A comparison of temperature changes of the protein spectra with temperature behavior of other systems with hydrogen bonds shows high thermostability of the functional active structure of protein molecules. The stability of proteins space organization is regulated and supported by non-monotonous temperature changes of this organization. The physical mechanism of thermostabilization includes interaction of hydrophobic radicals of protein with the aqueous environment.
Subject(s)
Hot Temperature , Protein Conformation , Protein Denaturation , Hydrogen-Ion Concentration , Models, Biological , SpectrophotometryABSTRACT
Temperature changes of protein infrared spectra have a nonmonotonous pattern. On the curves of temperature relationships of spectral characteristics the regions of high frequency displacement have been observed, interrupted by sharp low frequency shifts, partly or entirely compensating the displacement of the bands in the preceding temperature interval. It has been shown that at temperatures corresponding to the high frequency displacement heat weakening of the strength of hydrogen bonds takes place. At the low frequency shifts the whole system of the hydrogen bonds has an opposite change of the state maintaining high stability level of protein macromolecules in the broad temperature range.
Subject(s)
Serum Albumin, Bovine , Trypsin , Hydrogen Bonding , Protein Conformation , Protein Denaturation , Spectrophotometry, Infrared , TemperatureABSTRACT
The character of temperature changes of the absorption spectrum of water in protein solutions is the evidence of conformational changes of protein macromolecules. Along with the denaturation processes changes are also clearly seen at predenaturation stage. These changes involve a break of hydrophobic bonds in protein molecules and subsequent exponing of non-polar radicals into water. Thermodynamic characteristics of conformational changes of some proteins in aqueous solutions and water-organic mixtures are determined.
