Molecular effects of ozone on amino acids and proteins, especially human hemoglobin and albumin, and the need to personalize ozone concentration in major ozone autohemotherapy

臭氧 血红蛋白 化学 白蛋白 氨基酸 生物化学 环境化学 有机化学
作者
Fouad Mehraban,Arefeh Seyedarabi
出处
期刊:Critical Reviews in Clinical Laboratory Sciences [Informa]
卷期号:60 (5): 382-397 被引量:7
标识
DOI:10.1080/10408363.2023.2185765
摘要

AbstractAbstractMajor ozonated autohemotherapy is a complementary therapy that is widely used to treat various diseases. In the ozonation method, ozone that is dissolved in the plasma immediately reacts with biomolecules and produces H2O2 and lipid oxidation products (LOPs), which serve as ozone messengers/signaling molecules and result in the biological and therapeutic effects from ozonation. These signaling molecules affect hemoglobin and albumin, the most abundant proteins in red blood cells and plasma, respectively. Because hemoglobin and albumin perform important physiological functions, structural changes due to complementary therapeutic procedures and interventions such as major ozonated autohemotherapy at incorrect concentrations can lead to disruption of their functions. Oxidation reactions in hemoglobin and albumin can lead to unfavorable high molecular weight species, which can be prevented through personalized and correct use of ozone concentrations. In this review, we describe the molecular aspects of the effects of ozone on hemoglobin and albumin at inappropriate concentrations, which cause oxidation reactions that result in destructive effects; discuss the potential risks when ozonated blood is re-infused into the patient's blood stream in the process of major ozonated autohemotherapy; and emphasize the need for personalization of ozone concentrations.Keywords: Ozoneoxidationhuman hemoglobinhuman albuminpersonalizing ozone concentration AcknowledgmentsIt was not possible to write this article without benefiting from the studies conducted on the use of ozone on human hemoglobin and albumin samples in the Protein Structure and Function studies laboratory at the Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.Disclosure statementNo potential conflict of interest was reported by the author(s).Additional informationFundingThe author(s) reported there is no funding associated with the work featured in this article.
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