Detection of interactions of the β‐amyloid peptide with small molecules employing transferred NOEs |
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| Authors: | Dimitra Benaki Konstantina Stathopoulou Leondios Leondiadis Nikolaos Ferderigos Maria Pelecanou Emmanuel Mikros |
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| Affiliation: | 1. Institute of Biology, NCSR “Demokritos” 15310 Athens, Greece;2. Division of Pharmaceutical Chemistry, University of Athens, Panepistimiopolis, Zografou 15771, Athens, Greece;3. Mass Spectrometry and Dioxin Analysis Lab, Institute of Radioisotopes and Radiodiagnostic Products, NCSR “Demokritos” 15310 Athens, Greece;4. Division of Organic Chemistry, University of Athens, Panepistimiopolis, Zografou 15771 Athens, Greece |
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| Abstract: | The interaction of pineal hormone melatonin, the histological dye thioflavin T, and the olive tree polyphenol oleuropein, with the 28 amino acid residue N‐terminal fragment of the β‐amyloid peptide (β‐AP) of Alzheimer's disease, [β‐AP(1‐28)], was detected in solution through the observation of transferred NOEs (trNOEs) in 1D and 2D NOE spectroscopy (NOESY) experiments. The trNOE method is applied for the first time in the detection of interactions of soluble β‐AP(1‐28) with small molecules and may provide a means of screening for the identification of possible inhibitors of the formation of neurotoxic β‐AP assemblies. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd. |
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| Keywords: | β ‐amyloid peptide melatonin thioflavin T oleuropein transferred NOE |
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