Organic Base-Facilitated Thiol-Thioalkyne Reaction with Exclusive Regio- and Stereoselectivity.

Here, we report the regiospecific hydrothiolation of electron-rich thioalkynes with exclusive stereoselectivity facilitated by an organic base, which could proceed exceedingly fast under ambient atmosphere and room temperature, affording β addition products in up to nearly quantitative yields. The dual nature of the sulfur atom in attracting and donating electrons is supposed to be pivotal in determining the regio- and stereoselectivity. This system tolerates a wide range of thiols and thioalkynes and shows great potential in polymer synthesis.

Microenvironment Created by SnSe Vapor and Pre-Selenization to Stabilize the Surface and Back Contact in Kesterite Solar Cells.

The ambient air-processed preparation of kesterite Cu ZnSn(S,Se) (CZTSSe) thin film is highly promising for the fabrication of low-cost and eco-friendly solar cells. However, the Sn volatilization loss and formation of a thick Mo(S,Se) interfacial layer during the traditional selenization process pose challenges for fabricating high-efficiency CZTSSe solar cells. Here, CZTS precursors prepared by a sol-gel process in ambient air are selenized and assisted with SnSe vapor via one- and two-step selenization to prepare a CZTSSe absorber on a Mo film and, subsequently, solar cells.

Direct Observation of Native Silk Fibroin Conformation in Silk Gland of Silkworm.

To understand the natural silk spinning mechanism, synchrotron Fourier transform infrared (S-FTIR) microspectroscopy was employed in this study to monitor the conformation changes of silk protein in the silk gland of silkworm. The ultrahigh brightness of S-FTIR microspectroscopy allowed the imaging of the silk gland with micrometer-scale spatial resolution. Herein, tissue sections of a silk gland, including cross-section slices and longitudinal-section slices, were characterized.

Application of far-infrared spectroscopy to the structural identification of protein materials.

Although far-infrared (IR) spectroscopy has been shown to be a powerful tool to determine peptide structure and to detect structural transitions in peptides, it has been overlooked in the characterization of proteins. Herein, we used far-IR spectroscopy to monitor the structure of four abundant non-bioactive proteins, namely, soybean protein isolate (SPI), pea protein isolate (PPI) and two types of silk fibroins (SFs), domestic Bombyx mori and wild Antheraea pernyi. The two globular proteins SPI and PPI result in broad and weak far-IR bands (between 50 and 700 cm-1), in agreement with those of some other bioactive globular proteins previously studied (lysozyme, myoglobin, hemoglobin, etc.