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Methamphetamine binds to α‐synuclein and causes a conformational change which can be detected by nanopore analysis
Author(s) -
Tavassoly Omid,
Lee Jeremy S.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.040
Subject(s) - circular dichroism , methamphetamine , conformational change , alpha synuclein , chemistry , biophysics , dopaminergic , nanopore , drug , dementia with lewy bodies , parkinson's disease , biochemistry , disease , biology , medicine , dopamine , neuroscience , pharmacology , dementia , nanotechnology , materials science
α‐Synuclein is an intrinsically disordered protein of 140 amino acids which is abundant in dopaminergic neurons. Misfolding and aggregation of α‐synuclein leads to the formation of Lewy bodies inside the neurons which is the hallmark of Parkinson's disease and related dementias. Here we show by nanopore analysis that the recreational drug, methamphetamine, binds to the N‐terminus of α‐synuclein and causes a conformational change which cannot be detected by circular dichroism spectroscopy. The results suggest a mechanism for the psychoactivity of methamphetamine as well as an increased incidence of Parkinson's disease amongst users of the drug.