60912-44-9Relevant articles and documents
Anti-oligomerization sheet molecules: Design, synthesis and evaluation of inhibitory activities against α-synuclein aggregation
Liu, Hao,Chen, Li,Zhou, Fei,Zhang, Yun-Xiao,Xu, Ji,Xu, Meng,Bai, Su-Ping
supporting information, p. 3089 - 3096 (2019/06/14)
Aggregation of α-synuclein (α-Syn) play a key role in the development of Parkinson Disease (PD). One of the effective approaches is to stabilize the native, monomeric protein with suitable molecule ligands. We have designed and synthesized a series of sheet-like conjugated compounds which possess different skeletons and various heteroatoms in the two blocks located at both ends of linker, which have good π-electron delocalization and high ability of hydrogen-bond formation. They have shown anti-aggregation activities in vitro towards α-Syn with IC50 down to 1.09 μM. The molecule is found binding in parallel to the NACore within NAC domain of α-Syn, interfering aggregation of NAC region within different α-Syn monomer, and further inhibiting or slowing down the formation of α-Syn oligomer nuclei at lag phase. The potential inhibitor obtained by our strategy is considered to be highly efficient to inhibit α-Syn aggregation.
Supramolecular assembly in side-chain conjugated thiophene copolymers
Ananthakrishnan, Soundaram Jeevarathinam,Kumar, Balasubramaniyan Sambath,Somanathan, Narayanasastri,Mandal, Asit Baran
, p. 8331 - 8340 (2013/09/02)
Supramolecular assembly of side chain-conjugated polythiophenes were brought about by a interplay of dipole-dipole interactions and hydrogen bonding. Copolymers of (E)-3,5-dimethyl-4-(2-(thiophene-3-yl)vinyl) isoxazole (DTVI) and (E)-2-(2-(thiophen-3-yl)
Synthesis and in vitro evaluation of fluorinated styryl benzazoles as amyloid-probes
Ribeiro Morais, Goreti,Vicente Miranda, Hugo,Santos, Isabel C.,Santos, Isabel,Outeiro, Tiago F.,Paulo, Antonio
scheme or table, p. 7698 - 7710 (2012/01/03)
The formation of proteinaceous aggregates is a pathognomonic hallmark of several neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. To date, the final diagnostic for these diseases can only be achieved by immunostaining of post-mortem brain tissues with the commonly used congo red and Thioflavin T/S amyloid-dyes. The interest in developing amyloid-avid radioprobes to be used for protein aggregates imaging by positron emission tomography has grown substantialy, due to the promise in assisting diagnosis of these disorders. To this purpose, the present work describes the synthesis and characterization of four novel fluorinated styryl benzazole derivatives 1-4 by means of the Wittig reaction, as well as their in vitro evaluation as amyloid-probing agents. All compounds were obtained as mixtures of geometric E and Z isomers, with the preferable formation of the E isomer. Photoisomerization reactions allowed for the maximization of the minor Z isomers. The authentic 1-4E/Z isomers were isolated after purification by column chromatography under dark conditions. Profiting from the fluorescence properties of the different geometric isomers of 1-4, their binding affinities towards amyloid fibrils of insulin, α-synuclein and β-amyloid peptide were also measured. These compounds share similarities with Thioflavin T, interacting specifically with fibrillary species with a red-shift in the excitation wavelengths along with an increase in the fluorescence emission intensity. Apparent binding constants were determined and ranged between 1.22 and 23.96 μM-1. The present data suggest that the novel fluorinated styryl benzazole derivatives may prove useful for the design of 18F-labeled amyloid radioprobes.
