Improved Synthesis of Fluticasone Propionate

A novel process for the preparation of fluticasone propionate (<b>1</b>), a corticosteroid, is reported. In this paper, compound <b>2</b> was used as starting material to prepare <b>6</b> by using NaClO or NaBrO which was much cheaper than H₅IO₆ as an oxidizing agent. Furthermore, toxic, expensive, and pollutive BrCH₂F was replaced by AgNO₃ and Selectfluor in decarboxylative fluorination

Secondary structure prediction of hic31.

<p>Based on the protein sequence of hic22, the secondary structure prediction is performed by Phyre². The amino acids are colored based on the physiochemical properties of the side chains. The regions adopting putative α-helix and β-sheet conformations are represented as green spiral and blue arrow, respectively. The degrees of confidence 0.9 are also indicated by a rainbow color gradient.</p

cDNA and deduced amino acid sequence of hic31.

<p>The putative signal peptide is shown underlined. The putative polyadenylation signal (AATATA) is shown underlined boxed. The cDNA sequence of hic31 has been submitted to Genebank (Accession No. KR534872).</p

Detailed information about template in the secondary structure prediction.

<p>Detailed information about template in the secondary structure prediction.</p

The relative expression level of hic31 in the pearl sac during the early stages of pearl formation after implantation.

<p>The relative expression level of hic31 in the pearl sac during the early stages of pearl formation after implantation.</p

Amino acid composition (mole percent) of Hic31.

<p>Amino acid composition (mole percent) of Hic31.</p

<i>In situ</i> hybridization analysis of hic31 gene expression in the mantle of <i>Hyriopsis cumingii</i>.

<p>IF, inner fold; MF, middle fold; OF, outer fold.</p

Tissue-specific expression of hic31 by qRT-PCR.

<p>MM, Marginal mantle; VC, velum craspedon; CM, Center mantle; G, gill; H, hepatopancres; I, Intestine; K, kidney; AM, adductor muscle; F, Foot.</p

Three dimensional structure prediction of hic31.

<p>The tertiary structure prediction is performed by Phyre².</p

DataSheet_1_First genome assembly and annotation of Sanghuangporus weigelae uncovers its medicinal functions, metabolic pathways, and evolution.doc

Sanghuangporus, also known as “Sanghuang” in China, is a well-known genus of traditional Chinese medicinal macrofungi. To make more effective use of Sanghuangporus resources, we completed the first genome assembly and annotation of a monokaryon strain of S. weigelae in the present study. A 33.96-Mb genome sequence was assembled as 13 contigs, leading to prediction of 9377 protein-coding genes. Phylogenetic and average nucleotide identity analyses indicated that the S. weigelae genome is closely related to those of other Sanghuangporus species in evolutionary tree, which clustered in one clade. Collinearity analysis revealed a high level of collinearity of S. weigelae with S. baumii, S. vaninii, and S. sanghuang. Biosynthesis pathways potentially involved in medicinal properties, including terpenoid and polysaccharide synthesis, were identified in S. weigelae, while polysaccharides were identified as the main medicinal metabolites in S. weigelae, with flavonoids more important in Sanghuangporus than other medicinal mushroom groups. Genes encoding 332 carbohydrate-active enzymes were identified in the S. weigelae genome, including major glycoside hydrolases and glycosyltransferases predicted, revealing the robust lignocellulose degradation capacity of S. weigelae. Further, 130 genes, clustered in seven classes were annotated to encode cytochromes P450 in the S. weigelae genome. Overall, our results reveal the remarkably medicinal capacity of S. weigelae and provide new insights that will inform the study of evolution and medicinal application of S. weigelae. The data are a reference resource for the formulation of scientific and rational ecological protection policies for Sanghuangporus species.</p