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P4–263: Discovery of a regulatory site on beta–amyloid peptides
Author(s) -
Gadalla Moataz M.,
Hess George P.
Publication year - 2006
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2006.05.2002
Subject(s) - chemistry , binding site , peptide , aptamer , ligand (biochemistry) , biochemistry , receptor , nicotinic acetylcholine receptor , pharmacology , acetylcholine receptor , biophysics , microbiology and biotechnology , biology
Recently, RNA polymers (aptamers) were isolated [1] that bind to a beta-amyloid peptide with 40 residues [A (1-40)] that is associated with Alzheimer’s disease. We analyzed the published sequences and found a consensus sequence similar to that of inhibitory RNA Class I aptamers we had previously isolated. The RNA Class I aptamers bind to an inhibitory cocaine-binding site of the nicotinic acetylcholine receptor (nAChR) [2]. Whole-cell current recordings, using the rapid-reaction, cell-flow technique [3], indicate that, as hypothesized, the aptamer that binds to the amyloid peptide also inhibits the nAChR in a dose-dependent manner. As a consequence, we determined whether A (1-40) binds cocaine. Electrophoretic mobility shift assays indicated that it does.