Photophysical and DFT Characterization of Novel Pt(II)-Coupled 2,5-Diaryloxazoles for Nonlinear Optical Absorption

Several new bis-phosphine platinum­(II) complexes with 2,5-diaryl-substituted oxazole-containing alkyne ligands have been synthesized and optically characterized in solution. Measurements of nonlinear absorption showed strong attenuation of laser light at 532 and 600 nm. The light absorption of the Pt complexes was shifted from the near-UV region for the ground state to the red region for the excited triplet state, and was associated with large extinction coefficients. The optical limiting effect can be explained by triplet–triplet excited state absorption in conjunction with fast excited singlet–to-triplet intersystem crossing and slow triplet–to-ground-state decay, in comparison with the pulse length of the laser. DFT calculations show good predictability of the S₀–S₁ and S₀–T₁ energy gaps and offer insight into the interaction strength between Pt and the alkyne ligands. The use of this type of ligand, with weak absorption for the Pt­(II) complexes in the visual wavelength range as a key feature, enables the possibility to further improve these molecular systems for nonlinear absorption applications

Evidence for Age-Dependent <i>in Vivo</i> Conformational Rearrangement within Aβ Amyloid Deposits

Deposition of aggregated Aβ peptide in the brain is one of the major hallmarks of Alzheimer’s disease. Using a combination of two structurally different, but related, hypersensitive fluorescent amyloid markers, LCOs, reporting on separate ultrastructural elements, we show that conformational rearrangement occurs within Aβ plaques of transgenic mouse models as the animals age. This important mechanistic insight should aid the design and evaluation of experiments currently using plaque load as readout

Evidence for Age-Dependent <i>in Vivo</i> Conformational Rearrangement within Aβ Amyloid Deposits

Deposition of aggregated Aβ peptide in the brain is one of the major hallmarks of Alzheimer’s disease. Using a combination of two structurally different, but related, hypersensitive fluorescent amyloid markers, LCOs, reporting on separate ultrastructural elements, we show that conformational rearrangement occurs within Aβ plaques of transgenic mouse models as the animals age. This important mechanistic insight should aid the design and evaluation of experiments currently using plaque load as readout