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Linxiang Tan,Xiaoxia Ke,Xuechun Song,Qiaoqiao Yin,Ru Qiao,Kaiyan Guo,Lanlan Zhu 한국공업화학회 2018 Journal of Industrial and Engineering Chemistry Vol.60 No.-
A novel NIR-responsive photocatalyst NaYF4:Yb,Er@SiO2@Zn1 − xMnxO with double-layered core–shell structure was prepared by a three-step reaction. NaYF4:Yb,Er serves as a NIR-to-visible upconverter and provides “visible light” or “necessary energy” to Zn1 − xMnxO. Meanwhile, Mn2+-doping in Zn1 − xMnxO can extend the photoresponse of ZnO to visible-light region and enhance its charge separation. The nanocomposite exhibits good activity for dye decomposition and antibacterial property under NIR irradiation. The “energy absorption – energy conversion – energy transfer – surface reaction” process dominates the overall photocatalytic activity. Based on the standard MTT (abbr. for 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide) assay, NaYF4:Yb,Er@SiO2@Zn1 − xMnxO also exhibits good biocompatibility and low cytotoxicity with human umbilical vein endothelial cells (HUVEC) as model cells.
Linxiang Tan,Wenjie Wu,Qiaoqiao Yin,Xiaoxia Ke,Ru Qiao,Guoxiu Tong,Lanlan Zhu 한국공업화학회 2017 Journal of Industrial and Engineering Chemistry Vol.52 No.-
The dimer-type heterostructured Ag/Zn0.995Ni0.005O microspheres were prepared via two-stepmicrowave-assisted process, which exhibited stronger visible-light-activated antibacterial performancethan visible-light only, ZnO/Vis, Zn0.995Ni0.005O/Vis, or AgNPs/Vis. It is attributed to not only theinteraction of released metal ions with functional groups of vital enzymes and proteins, but also thecollapsing force of reactive oxygen species to the cells. Photoelectrochemical measurements show thatthe photogenerated charges of Ag/Zn0.995Ni0.005O possess longer lifetime and higher separation resultingfrom the synergistic effect between Ni and Ag, which leads to its superior visible-light-drivenantibacterial performance. Gram-negative bacteria are more effectively restrained by Ag/Zn0.995Ni0.005Othan Gram-positive bacteria because of structural difference between their cell walls.
Fu, Xinmiao,Shi, Xiaodong,Yin, Linxiang,Liu, Jiafeng,Joo, Keehyoung,Lee, Jooyoung,Chang, Zengyi American Society for Biochemistry and Molecular Bi 2013 The Journal of biological chemistry Vol.288 No.17
<P>As ubiquitous molecular chaperones, small heat shock proteins (sHSPs) are crucial for protein homeostasis. It is not clear why sHSPs are able to bind a wide spectrum of non-native substrate proteins and how such binding is enhanced by heat shock. Here, by utilizing a genetically incorporated photo-cross-linker (<I>p</I>-benzoyl-<SMALL>l</SMALL>-phenylalanine), we systematically characterized the substrate-binding residues in IbpB (a sHSP from <I>Escherichia coli</I>) in living cells over a wide spectrum of temperatures (from 20 to 50 °C). A total of 20 and 48 residues were identified at normal and heat shock temperatures, respectively. They are not necessarily hydrophobic and can be classified into three types: types I and II were activated at low and normal temperatures, respectively, and type III mediated oligomerization at low temperature but switched to substrate binding at heat shock temperature. In addition, substrate binding of IbpB in living cells began at temperatures as low as 25 °C and was further enhanced upon temperature elevation. Together, these <I>in vivo</I> data provide novel structural insights into the wide substrate spectrum of sHSPs and suggest that sHSP is able to hierarchically activate its multi-type substrate-binding residues and thus act as a robust chaperone in cells under fluctuating growth conditions.</P>