Fully Ambient-Processed Perovskite Film for Perovskite Solar Cells: Effect of Solvent Polarity on Lead Iodide

Fully ambient-processed and highly efficient methylammonium lead iodide (MAPbI₃) perovskite films are very desirable for industrial manufacturing of perovskite solar cells (PSCs). To date, most reported highly efficient MAPbI₃ PSCs rely on the fabrication of lead iodide (PbI₂) films inside the glovebox. Here we report a simple fabrication method using extra dry isopropanol (IPA100) for obtaining uniform and loosely packed PbI₂ film, which leads to a uniform and highly crystalline MAPbI₃ film under ambient conditions. Compared with recently reported results (10%–15%) using IPA treatment in the glovebox, we achieved over 16% efficiency of PSCs while fabricating perovskite films in fully ambient conditions. We have found the removal of even trace amounts of water from IPA to be a key factor for the successful ambient fabrication of PbI₂ films, as the high polarity of water negatively influences the crystallinity and morphology of the PbI₂ film

Expression of B3 cDNA is sufficient to induce typical mixed-field agglutination.

<p>A. The indicated K562 sublines were treated with sodium butyrate to induce erythroid differentiation. The cells were then incubated with anti-B antibody and cell agglutination was observed using a phase contrast microscope. B. The numbers of aggregation with the indicated number of cells/aggregate were counted. Histogram for the agglutination size distribution was shown. The data represent the mean ± S.D. of three independent experiments. P<0.001 by Kruskal-Wallis test.</p

2×2 table of the serology tests results.

<p>2×2 table of the serology tests results.</p

The B antigen expression for B and B₃ subtypes.

a<p>The data represent the mean ± S.D. (n = 10) for the indicated transfectants. The mean percentage of B antigen-expressing cells obtained from B101 was used as references and was defined as 100%.</p>*<p>Student t-test was used for statistically analysis with <i>p</i><0.01 when compared with B101.</p

Comparison of the nucleotide sequences spanning genomic regions that contain the crossing-over sites in Intron 3 of the three types of St^a alleles.

<p>E and F are newly identified types in this study. Numbering of the nucleotides starts at the first nucleotide of the Intron 3. The locations of each recombination site of St^a variants are boxed. Positions of the nucleotides that are different in ordinary glycophorin genes and the variants are indicated.</p

Flow cytometric analysis of B antigen expression.

<p>The indicated cell lines were treated with sodium butyrate for 48 h to induce erythroid differentiation. The cells were then incubated with FITC-conjugated BS-I Isolectin B4 from <i>Bandeiraea simplicifolia</i>. Flow cytometric analyses were then performed to determine the levels of surface B antigen expression. Representative histograms for the indicated sublines were shown. The FITC-derived fluorescent intensity was displayed on the x-axis on a logarithmic scale and the number of cells on the y-axis.</p

PCR primers used in this study, including their precise locations.

<p>*From Ref. <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0098166#pone.0098166-Shih1" target="_blank">[7]</a>.</p><p>**Originally designed.</p><p>***From Ref. <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0098166#pone.0098166-Palacajornsuk1" target="_blank">[13]</a>. IN:intron. EX:exon.</p

PCR programs used in this study.

<p>PCR programs used in this study.</p

Schematic representation of the B₃ transferase structure and its interaction with galactose residues.

<p>The schematic representation of the B glycosyltransferases is based on previous studies <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0037272#pone.0037272-Yamamoto2" target="_blank">[3]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0037272#pone.0037272-Seltsam1" target="_blank">[27]</a>. The relative location of the ABO transferase for the cytoplasmic tail, transmembrane domain, stem region, calalytic domain and the galactose residues are shown. The exons 1 to 7 of the <i>ABO</i> gene encoding for the different parts of the B glycosyltransferases are indicated. The B glycosyltransferases catalyze the final step of B antigen synthesis by transferring 1,3-D-galactose residues onto H determinants as the specific acceptor glycoconjugates. As to B₃, the lack of exon 3 corresponding to the transmembrane and stem region of B glycosyltransferase likely produces B₃ protein that is unstable and causes a decrease in B₃ protein expression. It is also likely that, due to the short stem region, B₃ protein is less flexible and can not efficiently transfer 1,3-D-galactose to the H protein.</p

RT-PCR of B1 and B3 transcripts.

<p>Buffy coat from the peripheral blood of B1 (n = 3) and B3 (n = 3) cases were subject to total RNA isolation. RT-PCR was then performed to obtain B1 and B3 full-length cDNA using the primer pair ABOF303 and B3R120. The PCR products were analyzed by agarose gel electorphoresis analysis.</p