Abstract
Beta amyloid (Aβ) aggregation has been characterized to be responsible for several amyloid diseases. Fourier transform infrared (FTIR) spectroscopy, fluorescence, and atomic force microscopy (AFM) are used to investigate induced changes in the secondary structure of Aβ upon thermal denaturation and interaction with propofol and L-arginine. Spectral analysis has revealed an effective static quenching for the intrinsic fluorescence of Aβ by propofol and l-arginine with binding constants of 2.81 × 102 M-1 for Aβ-propofol and 0.37 × 102 M-1 for Aβ-L-arginine. Fourier self-deconvolution (FSD) technique has been used to evaluate the relative intensity changes in the spectra of the component bands in the amide I and amide II regions at different ligand’s concentration in the protein complex. The analysis showed a decrease in the intensities of the parallel beta bands of propofol and L-arginine interactions with Aβ, accompanied with an increase in the antiparallel bands for the Aβ-propofol interaction and a decrease for the Aβ-l-arginine interaction. The relative increase in peaks’ intensities at 1694 cm-1 and 1531 cm-1 for the propofol interaction is linked to the formation of oligomers in the protein.
Highlights
AD (Alzheimer’s disease) is a wide spread brain disease among older people
Despite the general interest concerning oligomers toxicity compared to fibrils, there is a real need to understand the structure of these insoluble forms of Amyloid β-peptides (Aβ)
Some studies have shown that fibrillar Aβ was organized in a parallel β-sheet conformation while oligomeric Aβ were attributed to an antiparallel β-sheet structure [9]
Summary
AD (Alzheimer’s disease) is a wide spread brain disease among older people. The disease is characterized by theHow to cite this paper: Darwish, S.M., Aiaidah, S.Y., Khalid, I.M., Abuteir, M.M. and Qawasmi, L. (2015) Spectroscopic Investigations of β-Amyloid Interactions with Propofol and L-Arginine. Several studies have suggested that the accumulation of pathogenic amyloid-β (Aβ) assemblies in the brain can result in the dismantling of synapses, neuronal circuits and networks, which are associated with memory loss and cognitive decline [5]-[7]. In addition it has been reported that an imbalance between the formation rate and the clearance rate of Aβ deposits in the brain increases the progression of AD [8]. Some studies have shown that fibrillar Aβ was organized in a parallel β-sheet conformation while oligomeric Aβ were attributed to an antiparallel β-sheet structure [9]
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