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Despite of widespread abuse and the presence of vast data about ethanol’s adverse effects on behavior, brain morphology and physiology, molecular mechanism underlying deteriorating effects of chronic ethanol intoxication on the nervous system still remain elusive. The aim of the present study is revisiting the potential effects of adult alcohol insult and/or withdrawal on the protein, nucleic acids, and lipid profi les in the rat hippocampus by using Fourier Transform Infrared (FTIR) spectroscopy. It is a rapid, sensitive and non-disturbing technique which gives information about different functional groups belonging to biomolecules, simultaneously [Garip et al. (2007) Appl Spectrosc]. In the current study the rats were intragastrically administered ethanol at a dose increasing from 4.5 g to12 g/kg for 15 days and then the mean blood alcohol concentration was measured as 605.67 ± 36 mg/dl. FTIR results revealed an increase in the total content of proteins, lipids, as well as amino, fatty, and nucleic acids. Moreover, an increase in lipid disordering and a decrease in membrane fl uidity were obtained. Chronic ethanol intoxication was also found to cause an increase in random coil and aggregated β sheet content indicating structural changes in proteins, such as denaturation. Signifi cant variations in DNA and RNA conformation were observed. These molecular changes are discussed in terms of their potential effects on the neural function.
Membrane and tissue proteins in biological systems are diffi cult to be isolated and crystallized. In recent years, a low resolution technique, Fourier Transform Infrared (FTIR) spectroscopy, has been improved and proven to be a reliable tool to determine the secondary structure of proteins. Using this technique, it is possible to see protein bands directly from the spectra of tissues and membranes which allow us to obtain information about protein secondary structure. Generally the information is deduced by monitoring the amide I band, which is located between 1700–1600 cm-1. This band is the result of many overlapping individual peaks arising from different protein conformations, such as α-helix, β-sheet or turns. In the current study, using Neural Network (NN) method based on FTIR spectra [Severcan et al. (2004) Anal Biochem], the radiation, epilepsy and antioxidant-induced variations in the secondary structure of proteins in brain tissues and membranes were determined. The results showed that lipoic acid treatment revealed an unaltered protein secondary structure, while radiation caused a signifi cant increase in random coil structure and epilepsy led to a signifi cant decrease in β-sheet structure in rat brain tissue. This study confi rms that NN approach based on FTIR data is a fast and effective method to predict the secondary structure of proteins in different biological systems.
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