ABSTRACT Samples of human hemoglobin, bovine serum albumin, lysozyme and myoglobin were used as prototype of proteins to investigate their response to exposure to high frequency electromagnetic fields (HF-EMFs), in order to study possible application to the treatment of cancer. To this aim, Fourier-transform infrared spectroscopy was used in the infrared region. The most evident result which appeared after 3 h exposure to HF-EMFs was a significant increase in intensity of the Amide I band and of CH2 bending vibrations, showing that the proteins aligned toward the direction of the field. In addition, proteins’ unfolding and aggregation occurred after exposure to HF-EMFs. These findings can be explained assuming a resonance interaction between the natural frequencies of proteins and HF-EMFs, which can induce iperpolarization of cells. Given that cancerous tissues were found to have natural frequencies different from natural frequencies of normal tissues, we can hypothesize to irradiate cancerous tissues using EMFs at natural frequencies of cancer cells, causing resonant interaction with cellular membrane channels, inducing increasing of ions’ flux across cellular channels and damaging the cellular functions of cancer cells.

中文翻译：

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电磁场与蛋白质之间的共振相互作用：癌症治疗的可能起点

摘要 人类血红蛋白、牛血清白蛋白、溶菌酶和肌红蛋白样品被用作蛋白质的原型，以研究它们对暴露于高频电磁场 (HF-EMF) 的反应，以研究其在癌症治疗中的可能应用。为此，傅里叶变换红外光谱被用于红外区域。暴露于 HF-EMF 3 小时后出现的最明显结果是酰胺 I 带和 CH2 弯曲振动的强度显着增加，表明蛋白质向场方向排列。此外，暴露于 HF-EMF 后，蛋白质会发生解折叠和聚集。这些发现可以通过假设蛋白质的自然频率和 HF-EMF 之间的共振相互作用来解释，这可以诱导细胞的超极化。