The structures of the six-coordinate Fe(III) and Ga(III) complexes of the cyclic 6- and 7-membered hydroxamic acids PIPOH and AZEPOH found in several mixed-ligand siderophores are intermediate between the octahedron (OC) and the trigonal prism (T...
Methionine Capped Nanoparticles as Acetylcholinesterase Inhibitors
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The enzyme acetylcholinesterase (AChE) is adsorbed on the surface of silver and gold nanoparticles, which is confirmed by SEM and FTIR measurements. From SEM micrographs, the enzyme looks like a thin membrane around nanoparticles. FTIR spectra of Ag and Au @LM NPs in the presence of AChE match the spectra of bare AChE.
The silver and gold L-methionine capped nanoparticles (Ag and Au @LM NPs) were analyzed as prospective acetylcholinesterase (AChE) inhibitors to test their potential in the treatment of cognitive impairment in depression and Alzheimer's disease. The stability of NPs, and their ability to inhibit AChE were studied by UV-Vis and FTIR spectrophotometry. At the same time, TEM and SEM measurements, DLS, and zeta potential measurements were employed in the structural characterization of NPs. Nearly spherical, negatively charged Ag and Au @LM NPs, with 17 nm and 31 nm in diameter, respectively, showed moderate inhibitory potential toward AChE in the given frame of investigated concentrations. For both NPs IC50 is not reached. Furthermore, the adsorption of enzyme molecules on the surface of Ag and Au @LM NPs was demonstrated. Hence, our assumption is that inhibition of AChE is caused by blockage of the enzyme‘s active site due to the steric hindrance of NPs.Zum Volltext
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