Scientific Results

Single molecule tracking analysis reveals that the surface mobility of amyloid oligomers is driven by their conformational structure

Year: 2011

Authors: Calamai M., Pavone FS.

Autors Affiliation: University of Florence, European Laboratory for Nonlinear Spectroscopy (LENS), Sesto Fiorentino, Florence 50019, Italy

Abstract: Several models have been proposed to explain the cytotoxicity of A beta oligomers. The structural polymorphism of the oligomers can account for the various toxic effects observed. By combining the use of conformation-specific antibodies and single particle tracking techniques, we have investigated the mobility of individual A beta 1-42 oligomers on the plasma membrane of living cells. Distinct structural types of A beta 1-42 oligomers were labeled with two different conformation-specific antibodies. While both types of oligomers showed a heterogeneous dynamic behavior, their overall mobility was found to be significantly different. Conversely, we discovered that other amyloid oligomers sharing a similar conformation but composed of different peptides (amylin and prion Sup35NM) display dynamic behaviors comparable to those found for A beta 1-42 oligomers. This study provides evidence for a link between the quaternary structure and the membrane mobility of proteins, revealing that structurally analogous supramolecular assemblies diffuse similarly in cells.

Journal/Review: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Volume: 133 (31)      Pages from: 12001  to: 12008

More Information: The work was supported by the European Union Seventh Framework Programme (FF7/2007-2013) under grant agreements no. 228334 and PIEF-GA-2009-254791.
KeyWords: Conformational structures; Dynamic behaviors; Heterogeneous dynamics; Living cell; Membrane mobility; Quaternary structure; Single particle tracking; Single-molecule tracking; Structural polymorphisms; Structural type; Supramolecular assemblies; Surface mobility; Toxic effect, Antibodies; Cell membranes; Conformations; Glycoproteins, Oligomers, amyloid beta oligomer; oligomer; unclassified drug, article; cell membrane; chemical analysis; chemical structure; conformational transition; human; human cell; neuroblastoma cell; protein analysis; protein structure; surface property, Amyloid beta-Peptides; Humans; Particle Size; Peptide Fragments; Protein Conformation; Surface Properties; Tissue Distribution; Tumor Cells, Cultured
DOI: 10.1021/ja200951f

Citations: 22
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