By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Proteins have been presented. According to news reporting originating from Guwahati, India, by NewsRx correspondents, research stated, "Primaquine (Pq) metabolic products are responsible for drug-associated hemotoxicity and limit primaquine usage. Methemoglobin (MetHb)-Pq molecular modeling was used to identify the Pq binding pocket."
Our news editors obtained a quote from the research from the Indian Institute of Technology, "UPLC, mass spectrometry, and other indirect analytical methods were used to predict the metabolite. MetHb generation, development of oxidative stress, inhibition of antioxidant enzymes, and scanning electron microscope (SEM) were used to characterize the hemotoxic potentials of oxidized Pq (Pqox). MetHb binded Pq at the heme site with KD=6.4 ?M as evidenced by a difference spectroscopy study. MetHb oxidized Pq through a single e-transfer mechanism to form Pqox. The analysis of Pq from MetHb-H2O2 peroxidase reaction mixture gave peaks at m/z 300.53 and m/z 243.42, corresponding to the hydroxyl and desamino derivative of Pq, respectively. Similar peaks were absent in Pq or Pq incubated with H2O2 in the same buffer system. A robust increase in MetHb formation, reactive oxygen species generation, and inhibition of antioxidant enzymes were found in red blood cells (RBCs) exposed to Pqox compared with a parent drug molecule. The RBC membrane exhibited visible damages to plasma membrane (holes) as evidenced by SEM analysis of Pqox-exposed RBCs. The MetHb-H2O2 system transforms quiescent parent drug molecule to a highly reactive oxidative form to exhibit severe hemolysis. MetHb-H2O2-mediated Pq hemolytic potentiation that is sensitive to spin trap indicates the role of Pq* radical or other single e-species in the process."
According to the news editors, the research concluded: "The result suggests that MetHb incites the molecular property of the Pq and peroxidase inhibitors can be explored to control drug-associated toxicity."
For more information on this research see: Methemoglobin incites primaquine toxicity through single-electron oxidation and modification. Journal of Basic and Clinical Physiology and Pharmacology, 2013;24(2):105-14 (see also Proteins).
The news editors report that additional information may be obtained by contacting S.N. Balaji, Malaria Research Group, Dept. of Biotechnology, Indian Institute of Technology-Guwahati, Guwahati, Assam, India.
Keywords for this news article include: Asia, India, Guwahati, Hemeproteins, Methemoglobin.
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