3 years ago

Bioinorganic Chemistry of Parkinson’s Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length β-Synuclein Protein

Bioinorganic Chemistry of Parkinson’s Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length β-Synuclein Protein
Markus Zweckstetter, Marco C. Miotto, Liliana Quintanar, Mayra D. Pavese, Claudio O. Fernández, Christian Griesinger
In this work we performed a detailed structural characterization of the Cu(I) complexes with the full-length acetylated form of β-synuclein (AcβS). Our results show that AcβS binds Cu(I) with higher affinity than acetylated α-synuclein (AcαS); however, the formation of the high-affinity AcβS−Cu(I) complex does not promote the substantial increase in α-helix conformation seen for the AcαS−Cu(I) complex. The differences in conformational and dynamical properties are discussed here in terms of its physiological and pathological implications.

Publisher URL: http://dx.doi.org/10.1021/acs.inorgchem.7b01292

DOI: 10.1021/acs.inorgchem.7b01292

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