Upscaling efficient and stable perovskite layers is one of the most challenging issues in the commercialization of perovskite solar cells. Here, a lead halide–templated crystallization strategy is developed for printing formamidinium (FA)–cesium (Cs) lead triiodide perovskite films. High-quality large-area films are achieved through controlled nucleation and growth of a lead halide•N-methyl-2-pyrrolidone adduct that can react in situ with embedded FAI/CsI to directly form α-phase perovskite, sidestepping the phase transformation from δ-phase. A nonencapsulated device with 23% efficiency and excellent long-term thermal stability (at 85°C) in ambient air (~80% efficiency retention after 500 hours) is achieved with further addition of potassium hexafluorophosphate. The slot die–printed minimodules achieve champion efficiencies of 20.42% (certified efficiency 19.3%) and 19.54% with an active area of 17.1 and 65.0 square centimeters, respectively.

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Protein-nanoparticle interactions are important in biomedical applications of nanoparticles and for growing biosafety concerns about nanomaterials. In this study, the interactions of four plasma proteins, human serum albumin (HSA), myoglobin (MB), hemoglobin (HB), and trypsin (TRP), with Au and Ag nanoparticles were investigated by FT-IR spectroscopy. The secondary structure of thio-proteins changed with time during incubation with Au and Ag nanoparticles, but the secondary structures of non-thio-proteins remained unchanged. The incubation time for structural changes depended on the sulfur-metal bond energy; the stronger the sulfur-metal energy, the less the time needed. H/D exchange experiments revealed that protein-NP complexes with thio-proteins were less dynamic than free proteins. No measurable dynamic differences were found between free non-thio-proteins and the protein-Au (or Ag) nanoparticle complex. Therefore, the impact of covalent bonds on the protein structure is greater than that of the electrostatic force.