RT Journal Article
T1 Monitoring the Formation of Amyloid Oligomers Using Photoluminescence Anisotropy
A1 Jiang, Bo
A1 Aliyan, Amir
A1 Cook, Nathan P.
A1 Augustine, Andrea
A1 Bhak, Ghibom
A1 Maldonado, Rodrigo
A1 Smith McWilliams, Ashleigh D.
A1 Flores, Erick M.
A1 Mendez, Nicolas
A1 Shahnawaz, Mohammad
A1 Godoy, Fernando J.
A1 Montenegro García, Javier
A1 Moreno-Gonzalez, Ines
A1 Martí, Angel A.
AB The formation of oligomeric soluble aggregates is related to the toxicity of amyloid peptides and proteins. In this manuscript, we report the use of a ruthenium polypyridyl complex ([Ru(bpy)2(dpqp)]2+) to track the formation of amyloid oligomers at different times using photoluminescence anisotropy. This technique is sensitive to the rotational correlation time of the molecule under study, which is consequently related to the size of the molecule. [Ru(bpy)2(dpqp)]2+ presents anisotropy values of zero when free in solution (due to its rapid rotation and long lifetime) but larger values as the size and concentration of amyloid-β (Aβ) oligomers increase. Our assays show that Aβ forms oligomers immediately after the assay is started, reaching a steady state at ∼48 h. SDS–PAGE, DLS, and TEM were used to confirm and characterize the formation of oligomers. Our experiments show that the rate of formation for Aβ oligomers is temperature dependent, with faster rates as the temperature of the assay is increased. The probe was also effective in monitoring the formation of α-synuclein oligomers at different times
PB American Chemical Society
SN 0002-7863
YR 2019
FD 2019-10
LK http://hdl.handle.net/10347/19847
UL http://hdl.handle.net/10347/19847
LA eng
NO J. Am. Chem. Soc. 2019, 141, 39, 15605-15610
NO AAM thanks the Welch Foundation (Grant C-1743) and JM thanks AEI (SAF2017-89890-R), ERC (DYNAP-677786) and HFSP (RGY0066/2017) for financial support
DS Minerva
RD 22 abr 2026