Achieving large-area organic photovoltaic (OPV) modules with reasonable cost and performance is an important step toward commercialization. In this work, solution-processed conventional and inverted OPV modules with an area of 216 cm2 were fabricated by the blade coating method. Film uniformity was controlled by adjusting the fabrication parameters of the blade coating procedure. The influence of the concentration of the solutions of the interfacial materials on OPV module performance was investigated. For OPV modules based on the PM6:Y6 photoactive layer, a certificated power conversion efficiency (PCE) of 9.10% was achieved for the conventional OPV modules based on the TASiW-12 interfacial layer while a certificated PCE of 11.27% was achieved for the inverted OPV modules based on the polyethylenimine (PEI) interfacial layer. As for OPV modules based on a commercially available photoactive layer, PV-X Plus, a PCE of 8.52% was achieved in the inverted OPV modules. A halogen-free solvent, o-xylene, was used as the solvent for PV-X Plus, which makes the industrial production much more environmentally friendly.

Background HIV-1 pol, which encodes enzymes required for virus replication, is initially translated as a Gag-Pol fusion protein. Gag-Pol is incorporated into virions via interactions with Gag precursor Pr55gag. Protease (PR) embedded in Gag-Pol mediates the proteolytic processing of both Pr55gag and Gag-Pol during or soon after virus particle release from cells. Since efficient Gag-Pol viral incorporation depends on interaction with Pr55gag via its N-terminal Gag domain, the prevention of premature Gag cleavage may alleviate Gag-Pol packaging deficiencies associated with cleavage enhancement from PR. Results We engineered PR cleavage-blocking Gag mutations with the potential to significantly reduce Gag processing efficiency. Such mutations may mitigate the negative effects of enhanced PR activation on virus assembly and Gag-Pol packaging due to an RT dimerization enhancer or leucine zipper dimerization motif. When co-expressed with Pr55gag, we noted that enhanced PR activation resulted in reduced Gag-Pol cis or trans incorporation into Pr55gag particles, regardless of whether or not Gag cleavage sites within Gag-Pol were blocked. Conclusions Our data suggest that the amount of HIV-1 Gag-Pol or Pol viral incorporation is largely dependent on virus particle production, and that cleavage blocking in the Gag-Pol N-terminal Gag domain does not exert significant impacts on Pol packaging.

The ultraviolet (UV) part in the sunlight is known to cause most damage to organic photovoltaics (OPV). UV filters therefore can improve stability. The lifetime of the UV‐filtered OPV is determined by visible light. Herein, visible sunlight is divided into several bands and modeled by light‐emitting diodes to study the stability of ternary OPV. Poly[(2,6‐(4,8‐bis(5‐(2‐ethylhexyl‐3‐fluoro)thiophen‐2‐yl)‐benzo[1,2‐b:4,5‐b′]dithiophene))‐alt‐(5,5‐(1′,3′‐di‐2‐thienyl‐5′,7′‐bis(2‐ethylhexyl)benzo[1′,2′‐c:4′,5′‐c′]dithiophene‐4,8‐dione)] (PM6) is used as the donor. 2,2′‐((2Z,2′Z)‐((12,13‐bis(2‐ethylhexyl)‐3,9‐diundecyl‐12,13‐dihydro‐[1,2,5]thiadiazolo[3,4‐e]thieno[2",3″:4′,5′]thieno[2′,3′:4,5]pyrrolo[3,2‐g]thieno[2′,3′:4,5]thieno[3,2‐b]indole‐2,10‐diyl)bis(methanylylidene))bis(5,6‐difluoro‐3‐oxo‐2,3‐dihydro‐1H‐indene‐2,1‐diylidene))dimalononitrile (Y6) is used as the acceptor. Another polymer is added as the second donor to improve the stability. As expected, the deep and light blue bands dominate the decay under visible light. After about 1200 h of blue irradiation, the devices enter a relatively stable state up to 3000 h of tracking, in sharp contrast to the continuous decay under UV. No chemical reaction is observed under blue light. Years of outdoor lifetime for nonfullerene OPV are projected with the UV filter.

Background HIV-1 pol, which encodes enzymes required for virus replication, is initially translated as a Gag-Pol fusion protein. Gag-Pol is incorporated into virions via interactions with Gag precursor Pr55gag. Protease (PR) embedded in Gag-Pol mediates the proteolytic processing of both Pr55gag and Gag-Pol during or soon after virus particle release from cells. Since efficient Gag-Pol viral incorporation depends on interaction with Pr55gag via its N-terminal Gag domain, the prevention of premature Gag cleavage may alleviate Gag-Pol packaging deficiencies associated with cleavage enhancement from PR. Results We engineered PR cleavage-blocking Gag mutations with the potential to significantly reduce Gag processing efficiency. Such mutations may mitigate the negative effects of enhanced PR activation on virus assembly and Gag-Pol packaging due to an RT dimerization enhancer or leucine zipper dimerization motif. When co-expressed with Pr55gag, we noted that enhanced PR activation resulted in reduced Gag-Pol cis or trans incorporation into Pr55gag particles, regardless of whether or not Gag cleavage sites within Gag-Pol were blocked. Conclusion Our data suggest that the amount of HIV-1 Gag-Pol or Pol viral incorporation is largely dependent on virus particle production, and that cleavage blocking in the Gag-Pol N-terminal Gag domain does not exert significant impacts on Pol packaging.