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Detection of interactions of the β‐amyloid peptide with small molecules employing transferred NOEs
Author(s) -
Benaki Dimitra,
Stathopoulou Konstantina,
Leondiadis Leondios,
Ferderigos Nikolaos,
Pelecanou Maria,
Mikros Emmanuel
Publication year - 2009
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1138
Subject(s) - peptide , chemistry , thioflavin , biochemistry , oleuropein , molecule , stereochemistry , biophysics , alzheimer's disease , biology , medicine , organic chemistry , disease , antioxidant
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.