Customizable Organic Charge-Transfer Cocrystals for the Dual-Mode Optoelectronics in the NIR (II) Window.

Organic molecules have been regarded as ideal candidates for near-infrared (NIR) optoelectronic active materials due to their customizability and ease of large-scale production. However, constrained by the intricate molecular design and severe energy gap law, the realization of optoelectronic devices in the second near-infrared (NIR (II)) region with required narrow band gaps presents more challenges. Herein, we have originally proposed a cocrystal strategy that utilizes intermolecular charge-transfer interaction to drive the redshift of absorption and emission spectra of a series BFXTQ (X = 0, 1, 2, 4) cocrystals, resulting in the spectra located at NIR (II) window and reducing the optical bandgap to ∼0.98 eV. Significantly, these BFXTQ-based optoelectronic devices can exhibit dual-mode optoelectronic characteristics. An investigation of a series of BFXTQ-based photodetectors exhibits detectivity (D*) surpassing 1013 Jones at 375 to 1064 nm with a maximum of 1.76 × 1014 Jones at 1064 nm. Moreover, the radiative transition of CT excitons within the cocrystals triggers NIR emission over 1000 nm with a photoluminescence quantum yield (PLQY) of ∼4.6% as well as optical waveguide behavior with a low optical-loss coefficient of 0.0097 dB/µm at 950 nm. These results promote the advancement of an emerging cocrystal approach in micro/nanoscale NIR multifunctional optoelectronics.

Organic Cocrystal Alloys: From Three Primary Colors to Continuously Tunable Emission and Applications on Optical Waveguides and Displays.

Multicolor luminescence of organic fluorescent materials is an essential part of lighting and optical communication. However, the conventional construction of a multicolor luminescence system based on integrating multiple organic fluorescent materials of a single emission band remains complicated and to be improved. Herein, organic alloys (OAs) capable of full-color emission are synthesized based on charge transfer (CT) cocrystals. By adjusting the molar ratio of electron donors, the emission color of the OAs can be conveniently and continuously regulated in a wide visible range from blue (CIE: 0.187, 0.277), to green (CIE: 0.301, 0.550), and to red (CIE: 0.561, 0.435). The OAs show analogous 1D morphology with smooth surface, allowing for full-color waveguides with low optical-loss coefficient. Impressively, full-color optical displays are easily achieved through the OAs system with continuous emission, which shows promising applications in the field of optical display and promotes the development of organic photonics.

Pillararene-functionalized rhodium nanoparticles for efficient catalytic reduction and photothermal sterilization.

Pillar[5]arene-functionalized rhodium nanoparticles (Rh@CPA NPs) are first synthesized via a facile one-pot chemical reduction method. Rh@CPA NPs with good reusability and biocompatibility show excellent catalytic activities in reducing toxic nitrophenols and azo dyes, and also exhibit superior photothermal ablation capability towards Staphylococcus aureus under 808 nm laser irradiation. This work suggests that the supramolecular capping strategy could be used to construct novel hybrid materials for various applications.

In vitro Aggregation Ability of Five Commercially Available Aß42 peptide.

BACKGROUND: As the most basic material, synthetic human Amyloid-ß (1-42) (Aß42) peptide from different manufacturers have been widely used. Their aggregation ability is vital to the reliability, repeatability and comparability of studies on Aß42 physiology and pathology. However, it has not been evaluated and compared. OBJECTIVE: To analyze the consistency of the aggregation ability of 5 commercially available Aß42 peptide. METHODS: 5 Aß42 peptide represented as A, B, C, D and E were pretreated by HFIP. The pretreated Aß42 peptide were dissolved in Thioflavin T (ThT) solution, and their aggregation kinetics was monitored for 30 h with the aggregation kinetics test. Meanwhile, the pretreated peptide were aggregated in phosphate buffered saline. After aggregated for 12 h, they were detected by methods of ThT fluorescence, far-UV circular dichroism (CD), SDS-PAGE, western blot, and transmission electron microscopy (TEM), respectively. After aggregation for 8 h and 12 h, their cytotoxicity to SH-SY5Y cells was further evaluated using Cell Counting Kit-8. RESULTS: For aggregation kinetics, peptide A, C and E remained low level curves, while peptide B and D presented typical sigmoidal kinetics curves. In CD measurement, the aggregates of peptide B and D showed relatively high negative CD peaks with the height of -8.09 mdeg and -14.37 mdeg, while the height of peptide A, C and E was -1.04, -3.55, and -3.88. In ThT assay, relative fluorescence intensity of the aggregates of peptide B and D were 7.79 and 8.82, higher than 1.19, 1.71, and 2.70 of peptide A, C and E, respectively. In SDS-PAGE, all aggregates contained monomers and eleven polymers. Moreover, peptide B-E presented a trapezoidal distribution from dimers to trimers, and peptide A aggregated to dimers. By western blot, the bands of monomers remained in all aggregates. Furthermore, peptide B and D aggregated to dimers and trimers, peptide A and C only aggregated to dimers, and peptide E showed a strong band of trimers. By TEM, protofibrils were observed only in peptide B, while substantial spherical aggregates were formed in other peptide. Additionally, peptide B, D and E exhibited higher cytotoxicity after aggregated for 8 h, whereas peptide A, B and D presented relatively high cytotoxicity after 12-hour aggregation. CONCLUSION: Commercially available Aß42 peptide showed obvious differences in aggregation ability, which should arouse enough attention in the field of basic study related to Aß42. The aggregation ability evaluation with the various assay methods has some discrepancies, and it is highly urgent to establish a reasonable and uniform measurement strategy.

Content of anti-ß-amyloid42 oligomers antibodies in multiple batches from different immunoglobulin preparations.

Immunoglobulin preparations are one of the promising drugs for Alzheimer's disease (AD). Anti-ß-amyloid (Aß) oligomers antibodies in immunoglobulin preparations are considered to be critical for the therapeutic effect against Alzheimer's disease. However, the antibodies content in immunoglobulin preparations varies greatly. In order to determine which factor contributes to the difference of the antibodies content, the content of anti-Aß oligomers antibodies in multiple batches of immunoglobulin preparations from two manufacturers were measured by enzyme-linked immunosorbent assay. The results showed that no significant difference was found in the antibodies content among different bathes of normal immunoglobulin preparations prepared by the same process from the same manufacturer, whereas significant difference was found in the antibodies content between normal immunoglobulin preparations prepared by ethanol fractionation and those by chromatography process from the same manufacturer. In addition, significant variation existed in the antibodies content between normal immunoglobulin preparations and specific immunoglobulin preparations that are produced by plasma pool of immunized donors. Based on analysis of these results, the preparation process and raw plasma could be the main contributing factors affecting the content of anti-Aß oligomers antibodies in immunoglobulin preparations. This finding might help to develop AD-specific immunoglobulin preparation containing higher content of anti-Aß oligomers antibodies.

Effect of Different Aß Aggregates as Antigen on the Measure of Naturally Occurring Autoantibodies against Amyloid-ß40/42 in IVIG.

BACKGROUND: The specific Intravenous Immunoglobulin (IVIG) for Alzheimer's Disease (AD) is developing, which contains a high level of naturally occurring autoantibodies against amyloid-ß (nAbs-Aß), and the measure of nAbs-Aß content is greatly essential. Though Enzyme-Linked Immunosorbent Assay (ELISA) has been widely used in detecting the nAbs-Aß content, the impact of Aß aggregates species chosen as antigen in ELISA on this measure has not been evaluated. OBJECTIVE: To clarify the influence of different Aß40/42 aggregates as antigen during ELISA on the content of nAbs-Aß40/42 measured in IVIG. METHOD: Preparation of various Aß40/42 aggregates was performed by different aggregation solutions and various lengths of time, and analyzed by western blot. Different Aß40/42 aggregates as antigen were adopted to measure the nAbs-Aß40/42 content in IVIG by ELISA, and the control was carried out to reduce interference of nonspecific binding. The Bonferroni and Dunnett's T3 were used for statistical analysis. RESULTS: The duration for the formation of Aß40/42 aggregates had more effect on detecting nAbs-Aß40/42 content in IVIG than the aggregation solution. Higher content of nAbs-Aß40/42 in the same IVIG was displayed when measured with Aß40/42 aggregates at day 3, instead of at day 0.5 and day 7.0. The nAbs- Aß40/42 contents in the same IVIG measured with Aß40/42 aggregates prepared in different solutions were obviously different, but there was no significant regularity among them. CONCLUSION: The nAbs-Aß40/42 content in the same IVIG is significantly different when measured with Aß40/42 aggregated under different conditions. The nAbs-Aß40/42 content in IVIG by antigen-dependent measures, like ELISA, is uncertain.