Synchrotron Fourier transform infrared microspectroscopy (sFTIRM) analysis of Al-induced Alzheimer's disease in rat brain cortical tissue.

Aluminium (Al) is reported to promote beta amyloid (Aβ) aggregation, free radical production and disturb acetylcholine metabolism leading to cognitive dysfunction that are strongly associated with Alzheimer's disease (AD). Here we utilized synchrotron Fourier transform infrared microspectroscopy (sFTIRM) to analyse the fine structure of proteins and lipids in the rat cortical brain tissues in response to AlCl toxicity and Lepidium sativum (LS) treatment after 42 and 65 days. For statistical analysis, we used principal component analysis (PCA). Our results showed profusion of gauche rotomers form in membrane lipid acyl chains that increases the membrane fluidity and disorder only in AD group indicated by the detected sνCH band shift to higher frequency. All half bands width (HBW) values of the decomposed amide I band showed marked decrease in AD group compared to the other tested groups, together with an increase in the amounts of β-sheets (1641 cm) protein and random coil structure (1654 cm). These were indicated by a drastic increase in the percentage areas ratios of (1638 cm/1654 cm) and (1641 cm/1654 cm) that may be attributed to a stronger the hydrogen bonds that stabilize the protein conformational structure and/or the increase of the β-strand length due to misfolded Aβ formation in response to Al toxicity through transit phase/phases dominated by random coil structure. In curative group, LS treatment reversed these changes and restored the protein and lipid integrities. To conclude, sFTIRM is a powerful tool that shed light on the biomolecular structure of AD-like cortical brain tissue and considered the therapeutic potential of LS as a promising natural AD treatment.