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Insight into conformational modification of alpha‐synuclein in the presence of neuronal whole cells and of their isolated membranes
Author(s) -
Smaldone Giovanni,
Diana Donatella,
Pollegioni Loredano,
Di Gaetano Sonia,
Fattorusso Roberto,
Pedone Emilia
Publication year - 2015
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.2015.02.012
Subject(s) - alpha synuclein , membrane , biophysics , chemistry , conformational change , monomer , extracellular , fibril , biochemistry , microbiology and biotechnology , stereochemistry , biology , parkinson's disease , medicine , disease , organic chemistry , pathology , polymer
A change in the conformational plasticity of α‐Synuclein (α‐Syn) is hypothesised to be a key step in the pathogenic mechanism of Parkinson's disease (PD). Here, we report the study of extracellular α‐Syn interaction with whole cells and membranes isolated from the neuronal SH‐SY5Y cells, exploiting NMR and CD spectroscopies. In addition, the crosslinking agent DSG was used to freeze the conformational and oligomeric state of α‐Syn in the presence of cells. These data, in a quasi‐physiological environment, confirm the protein monomeric state with a propensity to adopt a transient alpha helical following interaction with biological membranes.